We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1w7a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1w7a.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1w7a.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1w7a| PDB=1w7a | SCENE= }}
{{STRUCTURE_1w7a| PDB=1w7a | SCENE= }}
-
'''ATP BOUND MUTS'''
+
===ATP BOUND MUTS===
-
==Overview==
+
<!--
-
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, showing increased affinity between the ATPase domains upon ATP binding and decreased affinity in the presence of ADP. Mutations of specific residues in the nucleotide-binding domain reduce the dimer affinity of the ATPase domains. In addition, ATP-induced release of DNA is strongly reduced in these mutants, suggesting that the two activities are coupled. Hence, it seems plausible that modulation of the affinity between ATPase domains is the driving force for conformational changes in the MutS dimer. These changes are driven by distinct amino acids in the nucleotide-binding site and form the basis for long-range interactions between the ATPase domains and DNA-binding domains and subsequent binding of MutL and initiation of mismatch repair.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15297450}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15297450 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15297450}}
==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Dna repair]]
[[Category: Dna repair]]
[[Category: Dna-binding]]
[[Category: Dna-binding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:15:23 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:43:44 2008''

Revision as of 10:43, 28 July 2008

Image:1w7a.png

Template:STRUCTURE 1w7a

ATP BOUND MUTS

Template:ABSTRACT PUBMED 15297450

About this Structure

1W7A is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Mon Jul 28 13:43:44 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1w7a"
Personal tools