1w7a: Difference between revisions
New page: left|200px<br /> <applet load="1w7a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w7a, resolution 2.27Å" /> '''ATP BOUND MUTS'''<b... |
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==About this Structure== | ==About this Structure== | ||
1W7A is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with MG and ATP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W7A OCA]]. | 1W7A is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with MG and ATP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W7A OCA]]. | ||
==Reference== | ==Reference== | ||
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[[Category: dna-binding]] | [[Category: dna-binding]] | ||
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Revision as of 15:14, 30 October 2007
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ATP BOUND MUTS
OverviewOverview
MutS is the key protein of the Escherichia coli DNA mismatch repair, system. It recognizes mispaired and unpaired bases and has intrinsic, ATPase activity. ATP binding after mismatch recognition by MutS serves as, a switch that enables MutL binding and the subsequent initiation of, mismatch repair. However, the mechanism of this switch is poorly, understood. We have investigated the effects of ATP binding on the MutS, structure. Crystallographic studies of ATP-soaked crystals of MutS show a, trapped intermediate, with ATP in the nucleotide-binding site. Local, rearrangements of several residues around the nucleotide-binding site, suggest a movement of the two ATPase domains of the MutS dimer toward each, other. Analytical ultracentrifugation experiments confirm such a, rearrangement, ... [(full description)]
About this StructureAbout this Structure
1W7A is a [Protein complex] structure of sequences from [Escherichia coli] with MG and ATP as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
ATP increases the affinity between MutS ATPase domains. Implications for ATP hydrolysis and conformational changes., Lamers MH, Georgijevic D, Lebbink JH, Winterwerp HH, Agianian B, de Wind N, Sixma TK, J Biol Chem. 2004 Oct 15;279(42):43879-85. Epub 2004 Aug 4. PMID:15297450
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