1u08
From Proteopedia
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Crystal Structure and Reactivity of YbdL from Escherichia coli Identify a Methionine Aminotransferase Function.
Overview
The ybdL gene of Escherichia coli codes for a protein of unknown function., Sequence analysis showed moderate homology to several vitamin B(6), dependent enzymes, suggesting that it may bind pyridoxal-5'-phosphate. The, structure analysis of YbdL to 2.35 A resolution by protein crystallography, verifies that it is a PLP dependent enzyme of fold type I, the typical, aspartate aminotransferase fold. The active site contains a bound, pyridoxal-5'-phosphate, covalently attached to the conserved active site, lysine residue Lys236. The pattern of conserved amino acids in the, putative substrate binding pocket of the enzyme reveals that it is most, closely related to a hyperthermophilic aromatic residue aminotransferase, from the archeon Pyrococcus horikoshii. Activity tests with 10 amino acids, as amino-donors reveal, however, a preference for Met, followed by His and, Phe, results which can be rationalized by modelization studies.
About this Structure
1U08 is a Single protein structure of sequence from Escherichia coli with PLP as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure and reactivity of YbdL from Escherichia coli identify a methionine aminotransferase function., Dolzan M, Johansson K, Roig-Zamboni V, Campanacci V, Tegoni M, Schneider G, Cambillau C, FEBS Lett. 2004 Jul 30;571(1-3):141-6. PMID:15280032
Page seeded by OCA on Wed Nov 21 03:44:29 2007
