1KQ7

E315Q Mutant Form of Fumarase C from E.coli

Summary for 1KQ7

• Entry DOI: 10.2210/pdb1kq7/pdb
• Related: 1FUO 1FUP 1FUQ 1FUR
• Descriptor: FUMARATE HYDRATASE CLASS II, D-MALATE, CITRIC ACID, ... (4 entities in total)
• Functional Keywords: fumarate lyase, lyase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm : P05042
• Total number of polymer chains: 2
• Total formula weight: 101613.91

Authors

Weaver, T.M.,Estevez, M.,Skarda, J.,Spencer, J. (deposition date: 2002-01-04, release date: 2002-08-23, Last modification date: 2023-08-16)

Primary citation

Estevez, M.,Skarda, J.,Spencer, J.,Banaszak, L.,Weaver, T.M.
X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation.
Protein Sci., 11:1552-1557, 2002

PubMed Abstract: 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.

PubMed: 12021453
DOI: 10.1110/ps.0201502

Experimental method

X-RAY DIFFRACTION (2.6 Å)