The structure of the C-C bond hydrolase MhpC provides insights into its catalytic mechanism.

doi:10.1016/j.jmb.2004.11.033

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Article

The structure of the C-C bond hydrolase MhpC provides insights into its catalytic mechanism.

Journal of molecular biology - 11 Feb 2005

Dunn G, Montgomery M G, Mohammed F, Coker A, Cooper J B, Robertson T, Garcia J-L, Bugg T D H, Wood S P

Abstract excerpt

2-Hydroxy-6-ketonona-2,4-diene-1,9-dioic acid 5,6-hydrolase (MhpC) is a 62 kDa homodimeric enzyme of the phenylpropionate degradation pathway of Escherichia coli. The 2.1 A resolution X-ray structure of the native enzyme determined from orthorhombic crystals confirms that it is a member of the alpha/beta hydrolase fold family, comprising eight beta-strands interconnected by loops and helices. The 2.8 A resolution...

Topics

Amino Acid Sequence
Binding Sites
Catalysis
Crystallography, X-Ray
Dimerization
Enzyme Inhibitors
Escherichia coli
Escherichia coli Proteins
Hydrolases
Models, Molecular
Molecular Sequence Data
Mutation
Protein Structure, Quaternary
Sequence Alignment

Source

Open in PubMed

Identifiers

PMID: 15663942
DOI: 10.1016/j.jmb.2004.11.033

Provenance

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