1ng9: Difference between revisions

Line 1:

[[Image:1ng9.~~gif~~|left|200px]]

[[Image:1ng9.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~E.coli MutS R697A: an ATPase-asymmetry mutant~~'''~~

===E.coli MutS R697A: an ATPase-asymmetry mutant===

~~==Overview==~~

<!--

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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_12554674}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12554674 is the PubMed ID number.

-->

==About this Structure==

Line 30:

Line 34:

[[Category: Dna binding]]

[[Category: Dna repair]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 02~~:29:40 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:22:17 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1ng9.gif|left|200px]]
+{{Seed}}
+[[Image:1ng9.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1ng9|  PDB=1ng9  |  SCENE=  }}
-'''E.coli MutS R697A: an ATPase-asymmetry mutant'''
+===E.coli MutS R697A: an ATPase-asymmetry mutant===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12554674}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12554674 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12554674}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Dna binding]]
 [[Category: Dna repair]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:29:40 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:22:17 2008''