1kq7
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(New page: 200px<br /><applet load="1kq7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kq7, resolution 2.60Å" /> '''E315Q Mutant Form of...)
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Revision as of 17:30, 20 November 2007
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E315Q Mutant Form of Fumarase C from E.coli
Overview
Fumarase catalyzes the reversible conversion of fumarate to S- malate, during the operation of the ubiquitous Kreb's cycle. Previous studies have, shown that the active site includes side chains from three of the four, subunits within the tetrameric enzyme. We used a clinically observed human, mutation to narrow our search for potential catalytic groups within the, fumarase active site. Offspring homozygous for the missense mutation, a, G-955-C transversion in the fumarase gene, results in the substitution of, a glutamine at amino acid 319 for the normal glutamic acid. To more fully, understand the implications of this mutation, a single-step site-directed, mutagenesis method was used to generate the homologous substitution at, position 315 within fumarase C from Escherichia coli. Subsequent kinetic, and X-ray crystal structure analyses show changes in the turnover number, and the cocrystal structure with bound citrate.
About this Structure
1KQ7 is a Single protein structure of sequence from Escherichia coli with MLT and CIT as ligands. Active as Fumarate hydratase, with EC number 4.2.1.2 Full crystallographic information is available from OCA.
Reference
X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation., Estevez M, Skarda J, Spencer J, Banaszak L, Weaver TM, Protein Sci. 2002 Jun;11(6):1552-7. PMID:12021453
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