1w7a

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m (Protected "1w7a" [edit=sysop:move=sysop])
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[[Image:1w7a.png|left|200px]]
 
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{{STRUCTURE_1w7a| PDB=1w7a | SCENE= }}
{{STRUCTURE_1w7a| PDB=1w7a | SCENE= }}
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===ATP BOUND MUTS===
===ATP BOUND MUTS===
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{{ABSTRACT_PUBMED_15297450}}
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==Function==
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[[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.
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{{ABSTRACT_PUBMED_15297450}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:015297450</ref><references group="xtra"/>
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<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

Template:STRUCTURE 1w7a

Contents

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

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OCA

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