1f44: Difference between revisions

Revision as of 02:39, 1 July 2008

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File:1f44.png

Template:STRUCTURE 1f44

CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEXCRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX

Template:ABSTRACT PUBMED 11601846

About this StructureAbout this Structure

1F44 is a Single protein structure of sequence from Enterobacteria phage p1. Full crystallographic information is available from OCA.

ReferenceReference

Quasi-equivalence in site-specific recombinase structure and function: crystal structure and activity of trimeric Cre recombinase bound to a three-way Lox DNA junction., Woods KC, Martin SS, Chu VC, Baldwin EP, J Mol Biol. 2001 Oct 12;313(1):49-69. PMID:11601846

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OCA

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 {{STRUCTURE_1f44|  PDB=1f44  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX'''
+===CRYSTAL STRUCTURE OF TRIMERIC CRE RECOMBINASE-LOX COMPLEX===
-==Overview==
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-The crystal structure of a novel Cre-Lox synapse was solved using phases from multiple isomorphous replacement and anomalous scattering, and refined to 2.05 A resolution. In this complex, a symmetric protein trimer is bound to a Y-shaped three-way DNA junction, a marked departure from the pseudo-4-fold symmetrical tetramer associated with Cre-mediated LoxP recombination. The three-way DNA junction was accommodated by a simple kink without significant distortion of the adjoining DNA duplexes. Although the mean angle between DNA arms in the Y and X structures was similar, adjacent Cre trimer subunits rotated 29 degrees relative to those in the tetramers. This rotation was accommodated at the protein-protein and DNA-DNA interfaces by interactions that are "quasi-equivalent" to those in the tetramer, analogous to packing differences of chemically identical viral subunits at non-equivalent positions in icosahedral capsids. This structural quasi-equivalence extends to function as Cre can bind to, cleave and perform strand transfer with a three-way Lox substrate. The structure explains the dual recognition of three and four-way junctions by site-specific recombinases as being due to shared structural features between the differently branched substrates and plasticity of the protein-protein interfaces. To our knowledge, this is the first direct demonstration of quasi-equivalence in both the assembly and function of an oligomeric enzyme.
+The line below this paragraph, {{ABSTRACT_PUBMED_11601846}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11601846 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_11601846}}
 ==About this Structure==
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 [[Category: Trimeric]]
 [[Category: Y-junction]]
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