1kq7

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{{STRUCTURE_1kq7| PDB=1kq7 | SCENE= }}
{{STRUCTURE_1kq7| PDB=1kq7 | SCENE= }}
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'''E315Q Mutant Form of Fumarase C from E.coli'''
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===E315Q Mutant Form of Fumarase C from E.coli===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12021453 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12021453}}
==About this Structure==
==About this Structure==
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[[Category: Weaver, T M.]]
[[Category: Weaver, T M.]]
[[Category: Fumarate lyase]]
[[Category: Fumarate lyase]]
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Revision as of 07:45, 2 July 2008

Template:STRUCTURE 1kq7

E315Q Mutant Form of Fumarase C from E.coli

Template:ABSTRACT PUBMED 12021453

About this Structure

1KQ7 is a Single protein structure of sequence from Escherichia coli. 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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