2pub: Difference between revisions

Revision as of 01:00, 28 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:2pub.png

Template:STRUCTURE 2pub

CRYSTAL STRUCTURE OF THE LACI FAMILY MEMBER, PURR, BOUND TO DNA: MINOR GROOVE BINDING BY ALPHA HELICESCRYSTAL STRUCTURE OF THE LACI FAMILY MEMBER, PURR, BOUND TO DNA: MINOR GROOVE BINDING BY ALPHA HELICES

Template:ABSTRACT PUBMED 7973627

About this StructureAbout this Structure

2PUB is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices., Schumacher MA, Choi KY, Zalkin H, Brennan RG, Science. 1994 Nov 4;266(5186):763-70. PMID:7973627

Page seeded by OCA on Mon Jul 28 01:00:17 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2pub.gif|left|200px]]
+{{Seed}}
+[[Image:2pub.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2pub|  PDB=2pub  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE LACI FAMILY MEMBER, PURR, BOUND TO DNA: MINOR GROOVE BINDING BY ALPHA HELICES'''
+===CRYSTAL STRUCTURE OF THE LACI FAMILY MEMBER, PURR, BOUND TO DNA: MINOR GROOVE BINDING BY ALPHA HELICES===
-==Overview==
+<!--
-The three-dimensional structure of a ternary complex of the purine repressor, PurR, bound to both its corepressor, hypoxanthine, and the 16-base pair purF operator site has been solved at 2.7 A resolution by x-ray crystallography. The bipartite structure of PurR consists of an amino-terminal DNA-binding domain and a larger carboxyl-terminal corepressor binding and dimerization domain that is similar to that of the bacterial periplasmic binding proteins. The DNA-binding domain contains a helix-turn-helix motif that makes base-specific contacts in the major groove of the DNA. Base contacts are also made by residues of symmetry-related alpha helices, the "hinge" helices, which bind deeply in the minor groove. Critical to hinge helix-minor groove binding is the intercalation of the side chains of Leu54 and its symmetry-related mate, Leu54', into the central CpG-base pair step. These residues thereby act as "leucine levers" to pry open the minor groove and kink the purF operator by 45 degrees.
+The line below this paragraph, {{ABSTRACT_PUBMED_7973627}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 7973627 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_7973627}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Zalkin, H.]]
 [[Category: Dna-binding regulatory protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 13:48:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 01:00:17 2008''