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The role of methionine 156 in cross-subunit nucleotide interactions in the iron protein of nitrogenase.

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Τίτλος: The role of methionine 156 in cross-subunit nucleotide interactions in the iron protein of nitrogenase.
Συγγραφείς: Bursey EH; Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697-3900, USA., Burgess BK
Πηγή: The Journal of biological chemistry [J Biol Chem] 1998 Nov 06; Vol. 273 (45), pp. 29678-85.
Τύπος έκδοσης: Journal Article; Research Support, U.S. Gov't, P.H.S.
Γλώσσα: English
Στοιχεία περιοδικού: Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print Cited Medium: Print ISSN: 0021-9258 (Print) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
Imprint Name(s): Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
Ιατρικοί όροι (MeSH): Oxidoreductases*, Adenosine Triphosphate/*metabolism , Methionine/*metabolism , Nitrogenase/*metabolism, Azotobacter vinelandii/enzymology ; Nitrogenase/chemistry ; Circular Dichroism ; Electron Spin Resonance Spectroscopy ; Hydrolysis ; Models, Molecular ; Protein Binding ; Protein Conformation ; Substrate Specificity
Περίληψη: A variant Fe protein has been created at the completely conserved residue methionine 156 by changing it to cysteine. The Azotobacter vinelandii strain expressing M156C is unable to grow under nitrogen-fixing conditions, and the purified protein cannot support substrate reduction in vitro. This mutation has an effect on the Fe protein's ability to undergo the MgATP-induced conformational change as evidenced by the fact that M156C is chelated in the presence of MgATP with a lower observed rate than wild-type. While the electron paramagnetic resonance spectra of this protein are similar to those of the wild-type Fe protein, the circular dichroism spectrum is markedly different in the presence of MgATP, showing that the conformation adopted by M156C following nucleotide binding is different from the wild-type conformation. Although competition activity and chelation assays show that this Fe protein can still form a complex with the MoFe protein, this altered conformation only supports MgATP hydrolysis at 1% the rate of wild-type Fe protein. A model based on x-ray crystallographic information is presented to explain the importance of Met-156 in stabilization of the correct conformation of the Fe protein via critical interactions of the residue with Asp-43 and nucleotide in the other subunit.
Grant Information: GM-45209 United States GM NIGMS NIH HHS
Substance Nomenclature: 8L70Q75FXE (Adenosine Triphosphate)
AE28F7PNPL (Methionine)
EC 1.- (Oxidoreductases)
EC 1.18.6.1 (Nitrogenase)
EC 1.18.6.1 (nitrogenase reductase)
Entry Date(s): Date Created: 19981029 Date Completed: 19981210 Latest Revision: 20210209
Update Code: 20260130
DOI: 10.1074/jbc.273.45.29678
PMID: 9792679
Βάση Δεδομένων: MEDLINE
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Items – Name: Title
  Label: Title
  Group: Ti
  Data: The role of methionine 156 in cross-subunit nucleotide interactions in the iron protein of nitrogenase.
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AU" term="%22Bursey+EH%22">Bursey EH</searchLink>; Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697-3900, USA.<br /><searchLink fieldCode="AU" term="%22Burgess+BK%22">Burgess BK</searchLink>
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  Data: <searchLink fieldCode="JN" term="%222985121R%22">The Journal of biological chemistry</searchLink> [J Biol Chem] 1998 Nov 06; Vol. 273 (45), pp. 29678-85.
– Name: TypePub
  Label: Publication Type
  Group: TypPub
  Data: Journal Article; Research Support, U.S. Gov't, P.H.S.
– Name: Language
  Label: Language
  Group: Lang
  Data: English
– Name: TitleSource
  Label: Journal Info
  Group: Src
  Data: <i>Publisher: </i><searchLink fieldCode="PB" term="%22Elsevier+Inc%2E+on+behalf+of+American+Society+for+Biochemistry+and+Molecular+Biology%22">Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology </searchLink><i>Country of Publication: </i>United States <i>NLM ID: </i>2985121R <i>Publication Model: </i>Print <i>Cited Medium: </i>Print <i>ISSN: </i>0021-9258 (Print) <i>Linking ISSN: </i><searchLink fieldCode="IS" term="%2200219258%22">00219258 </searchLink><i>NLM ISO Abbreviation: </i>J Biol Chem <i>Subsets: </i>MEDLINE
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  Label: Imprint Name(s)
  Group: PubInfo
  Data: <i>Publication</i>: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology<br /><i>Original Publication</i>: Baltimore, MD : American Society for Biochemistry and Molecular Biology
– Name: SubjectMESH
  Label: MeSH Terms
  Group: Su
  Data: <searchLink fieldCode="MM" term="%22Oxidoreductases%22">Oxidoreductases*</searchLink><br /><searchLink fieldCode="MM" term="%22Adenosine+Triphosphate%22">Adenosine Triphosphate</searchLink>/<searchLink fieldCode="MM" term="%22Adenosine+Triphosphate+metabolism%22">*metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Methionine%22">Methionine</searchLink>/<searchLink fieldCode="MM" term="%22Methionine+metabolism%22">*metabolism</searchLink> <br /><searchLink fieldCode="MM" term="%22Nitrogenase%22">Nitrogenase</searchLink>/<searchLink fieldCode="MM" term="%22Nitrogenase+metabolism%22">*metabolism</searchLink><br /><searchLink fieldCode="MH" term="%22Azotobacter+vinelandii%22">Azotobacter vinelandii</searchLink>/<searchLink fieldCode="MH" term="%22Azotobacter+vinelandii+enzymology%22">enzymology</searchLink> ; <searchLink fieldCode="MH" term="%22Nitrogenase%22">Nitrogenase</searchLink>/<searchLink fieldCode="MH" term="%22Nitrogenase+chemistry%22">chemistry</searchLink> ; <searchLink fieldCode="MH" term="%22Circular+Dichroism%22">Circular Dichroism</searchLink> ; <searchLink fieldCode="MH" term="%22Electron+Spin+Resonance+Spectroscopy%22">Electron Spin Resonance Spectroscopy</searchLink> ; <searchLink fieldCode="MH" term="%22Hydrolysis%22">Hydrolysis</searchLink> ; <searchLink fieldCode="MH" term="%22Models%2C+Molecular%22">Models, Molecular</searchLink> ; <searchLink fieldCode="MH" term="%22Protein+Binding%22">Protein Binding</searchLink> ; <searchLink fieldCode="MH" term="%22Protein+Conformation%22">Protein Conformation</searchLink> ; <searchLink fieldCode="MH" term="%22Substrate+Specificity%22">Substrate Specificity</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: A variant Fe protein has been created at the completely conserved residue methionine 156 by changing it to cysteine. The Azotobacter vinelandii strain expressing M156C is unable to grow under nitrogen-fixing conditions, and the purified protein cannot support substrate reduction in vitro. This mutation has an effect on the Fe protein's ability to undergo the MgATP-induced conformational change as evidenced by the fact that M156C is chelated in the presence of MgATP with a lower observed rate than wild-type. While the electron paramagnetic resonance spectra of this protein are similar to those of the wild-type Fe protein, the circular dichroism spectrum is markedly different in the presence of MgATP, showing that the conformation adopted by M156C following nucleotide binding is different from the wild-type conformation. Although competition activity and chelation assays show that this Fe protein can still form a complex with the MoFe protein, this altered conformation only supports MgATP hydrolysis at 1% the rate of wild-type Fe protein. A model based on x-ray crystallographic information is presented to explain the importance of Met-156 in stabilization of the correct conformation of the Fe protein via critical interactions of the residue with Asp-43 and nucleotide in the other subunit.
– Name: GrantInfo
  Label: Grant Information
  Group: Grant
  Data: GM-45209 United States GM NIGMS NIH HHS
– Name: NumberCAS
  Label: Substance Nomenclature
  Group: ID
  Data: 8L70Q75FXE (Adenosine Triphosphate)<br />AE28F7PNPL (Methionine)<br />EC 1.- (Oxidoreductases)<br />EC 1.18.6.1 (Nitrogenase)<br />EC 1.18.6.1 (nitrogenase reductase)
– Name: DateEntry
  Label: Entry Date(s)
  Group: Date
  Data: <i>Date Created: </i>19981029 <i>Date Completed: </i>19981210 <i>Latest Revision: </i>20210209
– Name: DateUpdate
  Label: Update Code
  Group: Date
  Data: 20260130
– Name: DOI
  Label: DOI
  Group: ID
  Data: 10.1074/jbc.273.45.29678
– Name: AN
  Label: PMID
  Group: ID
  Data: 9792679
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=cmedm&AN=9792679
RecordInfo BibRecord:
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    Identifiers:
      – Type: doi
        Value: 10.1074/jbc.273.45.29678
    Languages:
      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        StartPage: 29678
    Subjects:
      – SubjectFull: Azotobacter vinelandii enzymology
        Type: general
      – SubjectFull: Nitrogenase chemistry
        Type: general
      – SubjectFull: Circular Dichroism
        Type: general
      – SubjectFull: Electron Spin Resonance Spectroscopy
        Type: general
      – SubjectFull: Hydrolysis
        Type: general
      – SubjectFull: Models, Molecular
        Type: general
      – SubjectFull: Protein Binding
        Type: general
      – SubjectFull: Protein Conformation
        Type: general
      – SubjectFull: Substrate Specificity
        Type: general
      – SubjectFull: Oxidoreductases
        Type: general
      – SubjectFull: Adenosine Triphosphate metabolism
        Type: general
      – SubjectFull: Methionine metabolism
        Type: general
      – SubjectFull: Nitrogenase metabolism
        Type: general
    Titles:
      – TitleFull: The role of methionine 156 in cross-subunit nucleotide interactions in the iron protein of nitrogenase.
        Type: main
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          Name:
            NameFull: Bursey EH
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            NameFull: Burgess BK
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            – D: 06
              M: 11
              Text: 1998 Nov 06
              Type: published
              Y: 1998
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              Value: 45
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            – TitleFull: The Journal of biological chemistry
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