1baz: Difference between revisions

Revision as of 18:44, 30 June 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:1baz.png

Template:STRUCTURE 1baz

ARC REPRESSOR MUTANT PHE10VALARC REPRESSOR MUTANT PHE10VAL

Template:ABSTRACT PUBMED 9927650

About this StructureAbout this Structure

1BAZ is a Single protein structure of sequence from Enterobacteria phage p22. Full crystallographic information is available from OCA.

ReferenceReference

Origins of DNA-binding specificity: role of protein contacts with the DNA backbone., Schildbach JF, Karzai AW, Raumann BE, Sauer RT, Proc Natl Acad Sci U S A. 1999 Feb 2;96(3):811-7. PMID:9927650

Page seeded by OCA on Mon Jun 30 18:44:15 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1baz.gif|left|200px]]
+{{Seed}}
+[[Image:1baz.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1baz|  PDB=1baz  |  SCENE=  }}
-'''ARC REPRESSOR MUTANT PHE10VAL'''
+===ARC REPRESSOR MUTANT PHE10VAL===
-==Overview==
+<!--
-A central question in protein-DNA recognition is the origin of the specificity that permits binding to the correct site in the presence of excess, nonspecific DNA. In the P22 Arc repressor, the Phe-10 side chain is part of the hydrophobic core of the free protein but rotates out to pack against the sugar-phosphate backbone of the DNA in the repressor-operator complex. Characterization of a library of position 10 variants reveals that Phe is the only residue that results in fully active Arc. One class of mutants folds stably but binds operator with reduced affinity; another class is unstable. FV10, one member of the first class, binds operator DNA and nonoperator DNA almost equally well. The affinity differences between FV10 and wild type indicate that each Phe-10 side chain contributes 1.5-2.0 kcal to operator binding but less than 0.5 kcal/mol to nonoperator binding, demonstrating that contacts between Phe-10 and the operator DNA backbone contribute to binding specificity. This appears to be a direct contribution as the crystal structure of the FV10 dimer is similar to wild type and the Phe-10-DNA backbone interactions are the only contacts perturbed in the cocrystal structure of the FV10-operator complex.
+The line below this paragraph, {{ABSTRACT_PUBMED_9927650}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9927650 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9927650}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Schildbach, J F.]]
 [[Category: Transcription regulation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:17:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:44:15 2008''