Academic Journal
Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination.
| Τίτλος: | Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination. |
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| Συγγραφείς: | 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 |
| Πηγή: | 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. |
| Τύπος έκδοσης: | Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. |
| Γλώσσα: | English |
| Στοιχεία περιοδικού: | 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- |
| Ιατρικοί όροι (MeSH): | 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 |
| Περίληψη: | 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. |
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| 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 |
| Βάση Δεδομένων: | MEDLINE |
| ISSN: | 1744-3091 |
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| DOI: | 10.1107/S1744309106024791 |