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.

1nne

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1nne.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1nne.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1nne| PDB=1nne | SCENE= }}
{{STRUCTURE_1nne| PDB=1nne | SCENE= }}
-
'''Crystal Structure of the MutS-ADPBeF3-DNA complex'''
+
===Crystal Structure of the MutS-ADPBeF3-DNA complex===
-
==Overview==
+
<!--
-
During mismatch repair ATP binding and hydrolysis activities by the MutS family proteins are important for both mismatch recognition and for transducing mismatch recognition signals to downstream repair factors. Despite intensive efforts, a MutS.ATP.DNA complex has eluded crystallographic analysis. Searching for ATP analogs that strongly bound to Thermus aquaticus (Taq) MutS, we found that ADP.beryllium fluoride (ABF), acted as a strong inhibitor of several MutS family ATPases. Furthermore, ABF promoted the formation of a ternary complex containing the Saccharomyces cerevisiae MSH2.MSH6 and MLH1.PMS1 proteins bound to mismatch DNA but did not promote dissociation of MSH2.MSH6 from mismatch DNA. Crystallographic analysis of the Taq MutS.DNA.ABF complex indicated that although this complex was very similar to that of MutS.DNA.ADP, both ADP.Mg(2+) moieties in the MutS. DNA.ADP structure were replaced by ABF. Furthermore, a disordered region near the ATP-binding pocket in the MutS B subunit became traceable, whereas the equivalent region in the A subunit that interacts with the mismatched nucleotide remained disordered. Finally, the DNA binding domains of MutS together with the mismatched DNA were shifted upon binding of ABF. We hypothesize that the presence of ABF is communicated between the two MutS subunits through the contact between the ordered loop and Domain III in addition to the intra-subunit helical lever arm that links the ATPase and DNA binding domains.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12582174}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12582174 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12582174}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Yang, W.]]
[[Category: Yang, W.]]
[[Category: Dna]]
[[Category: Dna]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:44:45 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 02:36:28 2008''

Revision as of 23:36, 27 July 2008

Image:1nne.png

Template:STRUCTURE 1nne

Crystal Structure of the MutS-ADPBeF3-DNA complex

Template:ABSTRACT PUBMED 12582174

About this Structure

1NNE is a Single protein structure of sequence from Thermus aquaticus. Full crystallographic information is available from OCA.

Reference

Crystal structure and biochemical analysis of the MutS.ADP.beryllium fluoride complex suggests a conserved mechanism for ATP interactions in mismatch repair., Alani E, Lee JY, Schofield MJ, Kijas AW, Hsieh P, Yang W, J Biol Chem. 2003 May 2;278(18):16088-94. Epub 2003 Feb 11. PMID:12582174

Page seeded by OCA on Mon Jul 28 02:36:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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