1oh5: Difference between revisions

Revision as of 12:51, 10 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1oh5.png

Template:STRUCTURE 1oh5

THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A C:A MISMATCHTHE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A C:A MISMATCH

Template:ABSTRACT PUBMED 12907723

About this StructureAbout this Structure

1OH5 is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structures of Escherichia coli DNA mismatch repair enzyme MutS in complex with different mismatches: a common recognition mode for diverse substrates., Natrajan G, Lamers MH, Enzlin JH, Winterwerp HH, Perrakis A, Sixma TK, Nucleic Acids Res. 2003 Aug 15;31(16):4814-21. PMID:12907723

Page seeded by OCA on Thu Jul 10 12:51:48 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1oh5.gif|left|200px]]
+{{Seed}}
+[[Image:1oh5.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1oh5|  PDB=1oh5  |  SCENE=  }}
-'''THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A C:A MISMATCH'''
+===THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A C:A MISMATCH===
-==Overview==
+<!--
-We have refined a series of isomorphous crystal structures of the Escherichia coli DNA mismatch repair enzyme MutS in complex with G:T, A:A, C:A and G:G mismatches and also with a single unpaired thymidine. In all these structures, the DNA is kinked by approximately 60 degrees upon protein binding. Two residues widely conserved in the MutS family are involved in mismatch recognition. The phenylalanine, Phe 36, is seen stacking on one of the mismatched bases. The same base is also seen forming a hydrogen bond to the glutamate Glu 38. This hydrogen bond involves the N7 if the base stacking on Phe 36 is a purine and the N3 if it is a pyrimidine (thymine). Thus, MutS uses a common binding mode to recognize a wide range of mismatches.
+The line below this paragraph, {{ABSTRACT_PUBMED_12907723}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12907723 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12907723}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Dna binding]]
 [[Category: Mismatch recognition]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:50:26 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 10 12:51:48 2008''