1ng9: Difference between revisions
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[[Image:1ng9.gif|left|200px]] | [[Image:1ng9.gif|left|200px]] | ||
'''E.coli MutS R697A: an ATPase-asymmetry mutant''' | {{Structure | ||
|PDB= 1ng9 |SIZE=350|CAPTION= <scene name='initialview01'>1ng9</scene>, resolution 2.60Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | |||
|ACTIVITY= | |||
|GENE= MutS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''E.coli MutS R697A: an ATPase-asymmetry mutant''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1NG9 is a [ | 1NG9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NG9 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12554674 12554674] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: dna repair]] | [[Category: dna repair]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:56:30 2008'' | ||
Revision as of 13:56, 20 March 2008
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| , resolution 2.60Å | |||||||
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| Ligands: | and | ||||||
| Gene: | MutS (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
E.coli MutS R697A: an ATPase-asymmetry mutant
OverviewOverview
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.
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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