2v5k
From Proteopedia
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CLASS II ALDOLASE HPCH- MAGNESIUM- OXAMATE COMPLEX
Overview
Microorganisms are adept at degrading chemically resistant aromatic, compounds. One of the longest and most well characterized aromatic, catabolic pathways is the 4-hydroxyphenylacetic acid degradation pathway, of Escherichia coli. The final step involves the conversion of, 4-hydroxy-2-oxo-heptane-1,7-dioate into pyruvate and succinic, semialdehyde. This reaction is catalyzed by, 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (HpcH), a member of the, divalent metal ion dependent class II aldolase enzymes that have great, biosynthetic potential. We have solved the crystal structure of HpcH in, the apo form, and with magnesium and the substrate analogue oxamate bound, to 1.6 A and 2.0 A, respectively. Comparison with similar structures of, the homologous 2-dehydro-3-deoxygalactarate aldolase, coupled with, site-directed mutagenesis data, implicate histidine 45 and arginine 70 as, key catalytic residues.
About this Structure
2V5K is a Single protein structure of sequence from Escherichia coli with , and as ligands. Known structural/functional Sites: , , , , and . Full crystallographic information is available from OCA.
Reference
Structure and Mechanism of HpcH: A Metal Ion Dependent Class II Aldolase from the Homoprotocatechuate Degradation Pathway of Escherichia coli., Rea D, Fulop V, Bugg TD, Roper DI, J Mol Biol. 2007 Jun 26;. PMID:17881002
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