1dka
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(New page: 200px<br /><applet load="1dka" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dka, resolution 2.6Å" /> '''DIALKYLGLYCINE DECARB...)
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Revision as of 11:14, 20 November 2007
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DIALKYLGLYCINE DECARBOXYLASE STRUCTURE: BIFUNCTIONAL ACTIVE SITE AND ALKALI METAL BINDING SITES
Overview
The structure of the bifunctional, pyridoxal phosphate-dependent enzyme, dialkylglycine decarboxylase was determined to 2.1-angstrom resolution., Model building suggests that a single cleavage site catalyzes both, decarboxylation and transamination by maximizing stereoelectronic, advantages and providing electrostatic and general base catalysis. The, enzyme contains two binding sites for alkali metal ions. One is located, near the active site and accounts for the dependence of activity on, potassium ions. The other is located at the carboxyl terminus of an alpha, helix. These sites help show how proteins can specifically bind alkali, metals and how these ions can exert functional effects.
About this Structure
1DKA is a Single protein structure of sequence from Burkholderia cepacia with NA, K, PLP and MES as ligands. Active as 2,2-dialkylglycine decarboxylase (pyruvate), with EC number 4.1.1.64 Full crystallographic information is available from OCA.
Reference
Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sites., Toney MD, Hohenester E, Cowan SW, Jansonius JN, Science. 1993 Aug 6;261(5122):756-9. PMID:8342040
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