Source:http://linkedlifedata.com/resource/pubmed/id/11951047
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5566
|
| pubmed:dateCreated |
2002-4-12
|
| pubmed:databankReference | |
| pubmed:abstractText |
One of the most complex biosynthetic processes in metallobiochemistry is the assembly of nitrogenase, the key enzyme in biological nitrogen fixation. We describe here the crystal structure of an iron-molybdenum cofactor-deficient form of the nitrogenase MoFe protein, into which the cofactor is inserted in the final step of MoFe protein assembly. The MoFe protein folds as a heterotetramer containing two copies each of the homologous alpha and beta subunits. In this structure, one of the three alpha subunit domains exhibits a substantially changed conformation, whereas the rest of the protein remains essentially unchanged. A predominantly positively charged funnel is revealed; this funnel is of sufficient size to accommodate insertion of the negatively charged cofactor.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
1095-9203
|
| pubmed:author | |
| pubmed:issnType |
Electronic
|
| pubmed:day |
12
|
| pubmed:volume |
296
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
352-6
|
| pubmed:dateRevised |
2008-11-21
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| pubmed:meshHeading |
pubmed-meshheading:11951047-Amino Acid Sequence,
pubmed-meshheading:11951047-Azotobacter vinelandii,
pubmed-meshheading:11951047-Binding Sites,
pubmed-meshheading:11951047-Crystallization,
pubmed-meshheading:11951047-Crystallography, X-Ray,
pubmed-meshheading:11951047-Dimerization,
pubmed-meshheading:11951047-Hydrogen Bonding,
pubmed-meshheading:11951047-Models, Molecular,
pubmed-meshheading:11951047-Molecular Sequence Data,
pubmed-meshheading:11951047-Molybdoferredoxin,
pubmed-meshheading:11951047-Protein Conformation,
pubmed-meshheading:11951047-Protein Folding,
pubmed-meshheading:11951047-Protein Structure, Quaternary,
pubmed-meshheading:11951047-Protein Structure, Secondary,
pubmed-meshheading:11951047-Protein Structure, Tertiary,
pubmed-meshheading:11951047-Static Electricity,
pubmed-meshheading:11951047-Surface Properties
|
| pubmed:year |
2002
|
| pubmed:articleTitle |
Structure of a cofactor-deficient nitrogenase MoFe protein.
|
| pubmed:affiliation |
Division of Chemistry and Chemical Engineering, Mail Code 147-75CH, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|