1p4e: Difference between revisions

Revision as of 15:40, 27 July 2008

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File:1p4e.png

Template:STRUCTURE 1p4e

Flpe W330F mutant-DNA Holliday Junction ComplexFlpe W330F mutant-DNA Holliday Junction Complex

Template:ABSTRACT PUBMED 12716882

About this StructureAbout this Structure

1P4E is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

The role of the conserved Trp330 in Flp-mediated recombination. Functional and structural analysis., Chen Y, Rice PA, J Biol Chem. 2003 Jul 4;278(27):24800-7. Epub 2003 Apr 27. PMID:12716882

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-[[Image:1p4e.gif|left|200px]]
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 {{STRUCTURE_1p4e|  PDB=1p4e  |  SCENE=  }}
-'''Flpe W330F mutant-DNA Holliday Junction Complex'''
+===Flpe W330F mutant-DNA Holliday Junction Complex===
-==Overview==
+<!--
-The active site of Flp contains, in addition to a transdonated nucleophilic tyrosine, five other residues that are highly conserved within the lambda-integrase family of site-specific recombinases and the type IB topoisomerases. We have used site-directed mutagenesis and x-ray crystallography to investigate the roles of two such residues, Lys223 and Trp330. Our findings agree with studies on related enzymes showing the importance of Lys223 in catalysis but demonstrate that in Flp-mediated recombination the primary role of Trp330 is architectural rather than catalytic. Eliminating the hydrogen bonding potential of Trp330 by phenylalanine substitution results in surprisingly small changes in reaction rates, compared with dramatic decreases in the activities of W330A, W330H, and W330Q. The structure of a W330F mutant-DNA complex reveals an active site nearly identical to that of the wild type. The phenylalanine side chain preserves most of the van der Waals interactions Trp330 forms with the Tyr343-containing trans helix, which may be particularly important for the docking of this helix. Our studies of Trp330 provide the first detailed examination of this conserved residue in the lambda-integrase family, suggesting that the relative importance of active site residues may differ among Flp and related enzymes.
+The line below this paragraph, {{ABSTRACT_PUBMED_12716882}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12716882 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_12716882}}
 ==About this Structure==
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 [[Category: Site-specific recombination]]
 [[Category: W330]]
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