1ng9: Difference between revisions

Revision as of 19:22, 27 July 2008

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File:1ng9.png

Template:STRUCTURE 1ng9

E.coli MutS R697A: an ATPase-asymmetry mutantE.coli MutS R697A: an ATPase-asymmetry mutant

Template:ABSTRACT PUBMED 12554674

About this StructureAbout this Structure

1NG9 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

The alternating ATPase domains of MutS control DNA mismatch repair., Lamers MH, Winterwerp HH, Sixma TK, EMBO J. 2003 Feb 3;22(3):746-56. PMID:12554674

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OCA

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-'''E.coli MutS R697A: an ATPase-asymmetry mutant'''
+===E.coli MutS R697A: an ATPase-asymmetry mutant===
-==Overview==
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-DNA mismatch repair is an essential safeguard of genomic integrity by removing base mispairings that may arise from DNA polymerase errors or from homologous recombination between DNA strands. In Escherichia coli, the MutS enzyme recognizes mismatches and initiates repair. MutS has an intrinsic ATPase activity crucial for its function, but which is poorly understood. We show here that within the MutS homodimer, the two chemically identical ATPase sites have different affinities for ADP, and the two sites alternate in ATP hydrolysis. A single residue, Arg697, located at the interface of the two ATPase domains, controls the asymmetry. When mutated, the asymmetry is lost and mismatch repair in vivo is impaired. We propose that asymmetry of the ATPase domains is an essential feature of mismatch repair that controls the timing of the different steps in the repair cascade.
+The line below this paragraph, {{ABSTRACT_PUBMED_12554674}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12554674 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12554674}}
 ==About this Structure==
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 [[Category: Dna binding]]
 [[Category: Dna repair]]
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