1w7a: Difference between revisions
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{{STRUCTURE_1w7a| PDB=1w7a | SCENE= }} | {{STRUCTURE_1w7a| PDB=1w7a | SCENE= }} | ||
===ATP BOUND MUTS=== | ===ATP BOUND MUTS=== | ||
{{ABSTRACT_PUBMED_15297450}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/MUTS_ECOLI MUTS_ECOLI]] This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity. | |||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:015297450</ref><references group="xtra"/> | <ref group="xtra">PMID:015297450</ref><references group="xtra"/><references/> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Agianian, B.]] | [[Category: Agianian, B.]] | ||
Revision as of 08:40, 23 April 2014
ATP BOUND MUTS
Template:ABSTRACT PUBMED 15297450
Function
[MUTS_ECOLI] This protein is involved in the repair of mismatches in DNA. It is possible that it carries out the mismatch recognition step. This protein has a weak ATPase activity.
About this Structure
1w7a is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Lamers MH, Georgijevic D, Lebbink JH, Winterwerp HH, Agianian B, de Wind N, Sixma TK. ATP increases the affinity between MutS ATPase domains. Implications for ATP hydrolysis and conformational changes. J Biol Chem. 2004 Oct 15;279(42):43879-85. Epub 2004 Aug 4. PMID:15297450 doi:10.1074/jbc.M406380200