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Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination.

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Title: Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination.
Authors: Prabu JR; Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India., Thamotharan S, Khanduja JS, Alipio EZ, Kim CY, Waldo GS, Terwilliger TC, Segelke B, Lekin T, Toppani D, Hung LW, Yu M, Bursey E, Muniyappa K, Chandra NR, Vijayan M
Source: Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2006 Aug 01; Vol. 62 (Pt 8), pp. 731-4. Date of Electronic Publication: 2006 Jul 24.
Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
Language: English
Journal Info: Publisher: Wiley-Blackwell Country of Publication: England NLM ID: 101226117 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1744-3091 (Electronic) Linking ISSN: 17443091 NLM ISO Abbreviation: Acta Crystallogr Sect F Struct Biol Cryst Commun Subsets: MEDLINE
Imprint Name(s): Publication: Oxford, England : Wiley-Blackwell
Original Publication: Chester, England : International Union of Crystallography, c2005-
MeSH Terms: Recombination, Genetic*, Bacterial Proteins/*chemistry , Bacterial Proteins/*genetics , DNA Helicases/*chemistry , DNA Helicases/*genetics , Mycobacterium tuberculosis/*genetics, Binding Sites ; Crystallography, X-Ray ; Models, Molecular ; Protein Conformation
Abstract: The process of recombinational repair is crucial for maintaining genomic integrity and generating biological diversity. In association with RuvB and RuvC, RuvA plays a central role in processing and resolving Holliday junctions, which are a critical intermediate in homologous recombination. Here, the cloning, purification and structure determination of the RuvA protein from Mycobacterium tuberculosis (MtRuvA) are reported. Analysis of the structure and comparison with other known RuvA proteins reveal an octameric state with conserved subunit-subunit interaction surfaces, indicating the requirement of octamer formation for biological activity. A detailed analysis of plasticity in the RuvA molecules has led to insights into the invariant and variable regions, thus providing a framework for understanding regional flexibility in various aspects of RuvA function.
References: Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8257-62. (PMID: 10890893)
Microbiology. 2000 Sep;146 ( Pt 9):2093-5. (PMID: 10974096)
Nucleic Acids Res. 2000 Dec 15;28(24):4964-73. (PMID: 11121488)
Acta Crystallogr D Biol Crystallogr. 2002 Feb;58(Pt 2):195-208. (PMID: 11807243)
Mol Cell. 2002 Sep;10(3):671-81. (PMID: 12408833)
Proteins. 2003 Feb 15;50(3):474-85. (PMID: 12557189)
J Bacteriol. 2003 Jul;185(14):4280-4. (PMID: 12837805)
J Mol Biol. 2004 Jun 18;339(5):1103-13. (PMID: 15178251)
J Mol Biol. 2005 Jan 7;345(1):29-38. (PMID: 15567408)
Protein Expr Purif. 2005 May;41(1):207-34. (PMID: 15915565)
Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1140-8. (PMID: 16041080)
Nucleic Acids Res. 2006 Apr 28;34(8):2186-95. (PMID: 16648362)
Methods Enzymol. 1997;277:505-24. (PMID: 18488322)
Acta Crystallogr A. 1991 Mar 1;47 ( Pt 2):110-9. (PMID: 2025413)
Methods Enzymol. 1997;276:307-26. (PMID: 27754618)
Microbiol Rev. 1994 Sep;58(3):401-65. (PMID: 7968921)
J Bacteriol. 1996 Mar;178(5):1237-41. (PMID: 8631697)
Science. 1996 Oct 18;274(5286):415-21. (PMID: 8832889)
Mol Microbiol. 1996 Jul;21(2):205-11. (PMID: 8858576)
Trends Biochem Sci. 1996 Mar;21(3):107-11. (PMID: 8882584)
Structure. 1998 Jan 15;6(1):11-21. (PMID: 9493263)
J Mol Biol. 1998 Apr 24;278(1):105-16. (PMID: 9571037)
Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):905-21. (PMID: 9757107)
Mol Cell. 1998 Sep;2(3):361-72. (PMID: 9774974)
Molecular Sequence: PDB 2H5X
Substance Nomenclature: 0 (Bacterial Proteins)
EC 3.6.4.- (DNA Helicases)
Entry Date(s): Date Created: 20060802 Date Completed: 20060920 Latest Revision: 20181227
Update Code: 20260130
PubMed Central ID: PMC2242936
DOI: 10.1107/S1744309106024791
PMID: 16880543
Database: MEDLINE
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  Data: Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination.
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  Data: <searchLink fieldCode="AU" term="%22Prabu+JR%22">Prabu JR</searchLink>; Molecular Biophysics Unit, Indian Institute of Science, Bangalore, India.<br /><searchLink fieldCode="AU" term="%22Thamotharan+S%22">Thamotharan S</searchLink><br /><searchLink fieldCode="AU" term="%22Khanduja+JS%22">Khanduja JS</searchLink><br /><searchLink fieldCode="AU" term="%22Alipio+EZ%22">Alipio EZ</searchLink><br /><searchLink fieldCode="AU" term="%22Kim+CY%22">Kim CY</searchLink><br /><searchLink fieldCode="AU" term="%22Waldo+GS%22">Waldo GS</searchLink><br /><searchLink fieldCode="AU" term="%22Terwilliger+TC%22">Terwilliger TC</searchLink><br /><searchLink fieldCode="AU" term="%22Segelke+B%22">Segelke B</searchLink><br /><searchLink fieldCode="AU" term="%22Lekin+T%22">Lekin T</searchLink><br /><searchLink fieldCode="AU" term="%22Toppani+D%22">Toppani D</searchLink><br /><searchLink fieldCode="AU" term="%22Hung+LW%22">Hung LW</searchLink><br /><searchLink fieldCode="AU" term="%22Yu+M%22">Yu M</searchLink><br /><searchLink fieldCode="AU" term="%22Bursey+E%22">Bursey E</searchLink><br /><searchLink fieldCode="AU" term="%22Muniyappa+K%22">Muniyappa K</searchLink><br /><searchLink fieldCode="AU" term="%22Chandra+NR%22">Chandra NR</searchLink><br /><searchLink fieldCode="AU" term="%22Vijayan+M%22">Vijayan M</searchLink>
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  Data: <searchLink fieldCode="JN" term="%22101226117%22">Acta crystallographica. Section F, Structural biology and crystallization communications</searchLink> [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2006 Aug 01; Vol. 62 (Pt 8), pp. 731-4. <i>Date of Electronic Publication: </i>2006 Jul 24.
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  Data: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
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  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Wiley-Blackwell%22">Wiley-Blackwell </searchLink><i>Country of Publication: </i>England <i>NLM ID: </i>101226117 <i>Publication Model: </i>Print-Electronic <i>Cited Medium: </i>Internet <i>ISSN: </i>1744-3091 (Electronic) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2217443091%22">17443091 </searchLink><i>NLM ISO Abbreviation: </i>Acta Crystallogr Sect F Struct Biol Cryst Commun <i>Subsets: </i>MEDLINE
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  Data: <i>Publication</i>: Oxford, England : Wiley-Blackwell<br /><i>Original Publication</i>: Chester, England : International Union of Crystallography, c2005-
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  Group: Su
  Data: <searchLink fieldCode="MM" term="%22Recombination%2C+Genetic%22">Recombination, Genetic*</searchLink><br /><searchLink fieldCode="MM" term="%22Bacterial+Proteins%22">Bacterial Proteins</searchLink>/<searchLink fieldCode="MM" term="%22Bacterial+Proteins+chemistry%22">*chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22Bacterial+Proteins%22">Bacterial Proteins</searchLink>/<searchLink fieldCode="MM" term="%22Bacterial+Proteins+genetics%22">*genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22DNA+Helicases%22">DNA Helicases</searchLink>/<searchLink fieldCode="MM" term="%22DNA+Helicases+chemistry%22">*chemistry</searchLink> <br /><searchLink fieldCode="MM" term="%22DNA+Helicases%22">DNA Helicases</searchLink>/<searchLink fieldCode="MM" term="%22DNA+Helicases+genetics%22">*genetics</searchLink> <br /><searchLink fieldCode="MM" term="%22Mycobacterium+tuberculosis%22">Mycobacterium tuberculosis</searchLink>/<searchLink fieldCode="MM" term="%22Mycobacterium+tuberculosis+genetics%22">*genetics</searchLink><br /><searchLink fieldCode="MH" term="%22Binding+Sites%22">Binding Sites</searchLink> ; <searchLink fieldCode="MH" term="%22Crystallography%2C+X-Ray%22">Crystallography, X-Ray</searchLink> ; <searchLink fieldCode="MH" term="%22Models%2C+Molecular%22">Models, Molecular</searchLink> ; <searchLink fieldCode="MH" term="%22Protein+Conformation%22">Protein Conformation</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: The process of recombinational repair is crucial for maintaining genomic integrity and generating biological diversity. In association with RuvB and RuvC, RuvA plays a central role in processing and resolving Holliday junctions, which are a critical intermediate in homologous recombination. Here, the cloning, purification and structure determination of the RuvA protein from Mycobacterium tuberculosis (MtRuvA) are reported. Analysis of the structure and comparison with other known RuvA proteins reveal an octameric state with conserved subunit-subunit interaction surfaces, indicating the requirement of octamer formation for biological activity. A detailed analysis of plasticity in the RuvA molecules has led to insights into the invariant and variable regions, thus providing a framework for understanding regional flexibility in various aspects of RuvA function.
– Name: Ref
  Label: References
  Group: RefInfo
  Data: Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8257-62. (PMID: <searchLink fieldCode="PM" term="%2210890893%22">10890893)</searchLink><br />Microbiology. 2000 Sep;146 ( Pt 9):2093-5. (PMID: <searchLink fieldCode="PM" term="%2210974096%22">10974096)</searchLink><br />Nucleic Acids Res. 2000 Dec 15;28(24):4964-73. (PMID: <searchLink fieldCode="PM" term="%2211121488%22">11121488)</searchLink><br />Acta Crystallogr D Biol Crystallogr. 2002 Feb;58(Pt 2):195-208. (PMID: <searchLink fieldCode="PM" term="%2211807243%22">11807243)</searchLink><br />Mol Cell. 2002 Sep;10(3):671-81. (PMID: <searchLink fieldCode="PM" term="%2212408833%22">12408833)</searchLink><br />Proteins. 2003 Feb 15;50(3):474-85. (PMID: <searchLink fieldCode="PM" term="%2212557189%22">12557189)</searchLink><br />J Bacteriol. 2003 Jul;185(14):4280-4. (PMID: <searchLink fieldCode="PM" term="%2212837805%22">12837805)</searchLink><br />J Mol Biol. 2004 Jun 18;339(5):1103-13. (PMID: <searchLink fieldCode="PM" term="%2215178251%22">15178251)</searchLink><br />J Mol Biol. 2005 Jan 7;345(1):29-38. (PMID: <searchLink fieldCode="PM" term="%2215567408%22">15567408)</searchLink><br />Protein Expr Purif. 2005 May;41(1):207-34. (PMID: <searchLink fieldCode="PM" term="%2215915565%22">15915565)</searchLink><br />Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1140-8. (PMID: <searchLink fieldCode="PM" term="%2216041080%22">16041080)</searchLink><br />Nucleic Acids Res. 2006 Apr 28;34(8):2186-95. (PMID: <searchLink fieldCode="PM" term="%2216648362%22">16648362)</searchLink><br />Methods Enzymol. 1997;277:505-24. (PMID: <searchLink fieldCode="PM" term="%2218488322%22">18488322)</searchLink><br />Acta Crystallogr A. 1991 Mar 1;47 ( Pt 2):110-9. (PMID: <searchLink fieldCode="PM" term="%222025413%22">2025413)</searchLink><br />Methods Enzymol. 1997;276:307-26. (PMID: <searchLink fieldCode="PM" term="%2227754618%22">27754618)</searchLink><br />Microbiol Rev. 1994 Sep;58(3):401-65. (PMID: <searchLink fieldCode="PM" term="%227968921%22">7968921)</searchLink><br />J Bacteriol. 1996 Mar;178(5):1237-41. (PMID: <searchLink fieldCode="PM" term="%228631697%22">8631697)</searchLink><br />Science. 1996 Oct 18;274(5286):415-21. (PMID: <searchLink fieldCode="PM" term="%228832889%22">8832889)</searchLink><br />Mol Microbiol. 1996 Jul;21(2):205-11. (PMID: <searchLink fieldCode="PM" term="%228858576%22">8858576)</searchLink><br />Trends Biochem Sci. 1996 Mar;21(3):107-11. (PMID: <searchLink fieldCode="PM" term="%228882584%22">8882584)</searchLink><br />Structure. 1998 Jan 15;6(1):11-21. (PMID: <searchLink fieldCode="PM" term="%229493263%22">9493263)</searchLink><br />J Mol Biol. 1998 Apr 24;278(1):105-16. (PMID: <searchLink fieldCode="PM" term="%229571037%22">9571037)</searchLink><br />Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):905-21. (PMID: <searchLink fieldCode="PM" term="%229757107%22">9757107)</searchLink><br />Mol Cell. 1998 Sep;2(3):361-72. (PMID: <searchLink fieldCode="PM" term="%229774974%22">9774974)</searchLink>
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        Text: English
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        StartPage: 731
    Subjects:
      – SubjectFull: Binding Sites
        Type: general
      – SubjectFull: Crystallography, X-Ray
        Type: general
      – SubjectFull: Models, Molecular
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      – SubjectFull: Protein Conformation
        Type: general
      – SubjectFull: Recombination, Genetic
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      – SubjectFull: DNA Helicases chemistry
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      – SubjectFull: DNA Helicases genetics
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      – SubjectFull: Mycobacterium tuberculosis genetics
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      – TitleFull: Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination.
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