1ng9

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{{STRUCTURE_1ng9| PDB=1ng9 | SCENE= }}
{{STRUCTURE_1ng9| PDB=1ng9 | SCENE= }}
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'''E.coli MutS R697A: an ATPase-asymmetry mutant'''
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===E.coli MutS R697A: an ATPase-asymmetry mutant===
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==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.
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(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==
==About this Structure==
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[[Category: Dna binding]]
[[Category: Dna binding]]
[[Category: Dna repair]]
[[Category: Dna repair]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:29:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:22:17 2008''

Revision as of 16:22, 27 July 2008

Image:1ng9.png

Template:STRUCTURE 1ng9

E.coli MutS R697A: an ATPase-asymmetry mutant

Template:ABSTRACT PUBMED 12554674

About this Structure

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

Reference

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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