1sft
From Proteopedia
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ALANINE RACEMASE
Overview
The molecular structure of alanine racemase from Bacillus, stearothermophilus was determined by X-ray crystallography to a resolution, of 1.9 A. The alanine racemase monomer is composed of two domains, an, eight-stranded alpha/beta barrel at the N-terminus, which includes, residues 1-240, and a C-terminal domain essentially composed of, beta-strand (residues 241-388). In the structure of the dimer the mouth of, the alpha/beta barrel of one monomer faces the second domain of the other, monomer. The pyridoxal 5'-phosphate (PLP) cofactor lies in and above the, mouth of the alpha/beta barrel and is covalently linked via an aldimine, linkage to Lys39, which is at the C-terminus of the first beta-strand of, the alpha/beta barrel. This is the first example of a PLP cofactor binding, in the active site of a alpha/beta barrel. A number of other residues are, involved in maintaining the position of the PLP in the protein. Of these, Arg219 is the most interesting, as it forms a hydrogen bond with the, pyridine nitrogen of the cofactor. This is the first known occurrence of, such an interaction with PLP and is expected to influence the electron, delocalization in the PLP-alanine intermediates. A second arginine, residue, Arg136, donates a hydrogen bond to the phenolic oxygen of PLP and, may be involved in the binding of substrate as well as stabilization of, intermediates. Finally, Tyr265', from the second monomer, is postulated to, be 2 proton donor to the carbanion intermediate.
About this Structure
1SFT is a Single protein structure of sequence from Geobacillus stearothermophilus with ACT and PLP as ligands. Active as Alanine racemase, with EC number 5.1.1.1 Full crystallographic information is available from OCA.
Reference
Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution., Shaw JP, Petsko GA, Ringe D, Biochemistry. 1997 Feb 11;36(6):1329-42. PMID:9063881
Page seeded by OCA on Wed Nov 21 02:21:27 2007
