1vfh

Crystal structure of alanine racemase from D-cycloserine producing Streptomyces lavendulae

spinqualitylabelsall models 1vfh, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1vfh is a 1 chain structure with sequence from "actinomyces_lavendulae"_waksman_and_curtis_1916 "actinomyces lavendulae" waksman and curtis 1916. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PLP NonStd Res: KCX Related: 1vfs, 1vft Gene: alr ("Actinomyces lavendulae" Waksman and Curtis 1916) Activity: Alanine racemase, with EC number 5.1.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q65YW7_STRLA] Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids (By similarity).[HAMAP-Rule:MF_01201] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Alanine racemase (ALR), an enzyme that catalyzes the interconversion of Ala enantiomers, is essential for the synthesis of the bacterial cell wall. We have shown that it is harder to inhibit the catalytic activity of ALR from D-cycloserine (DCS)-producing Streptomyces lavendulae than that from Escherichia coli by DCS. To obtain structural evidence for the fact that Streptomyces ALR displays resistance to DCS, we determined the precise nature of the x-ray crystal structures of the cycloserine-free and cycloserine enantiomer-bound forms of Streptomyces ALR at high resolutions. Streptomyces ALR takes a dimer structure, which is formed by interactions between the N-terminal domain of one monomer with the C-terminal domain of its partner. Each of the two active sites of ALR, which is generated as a result of the formation of the dimer structure, is composed of pyridoxal 5'-phosphate (PLP), the PLP-binding residue Lys(38), and the amino acids in the immediate environment of the pyridoxal cofactor. The current model suggests that each active site of Streptomyces ALR maintains a larger space and takes a more rigid conformation than that of Bacillus stearothermophilus ALR determined previously. Furthermore, we show that Streptomyces ALR results in a slow conversion to a final form of a pyridoxal derivative arising from either isomer of cycloserine, which inhibits the catalytic activity noncompetitively. In fact, the slow conversion is confirmed by the fact that each enzyme bound cycloserine derivative, which is bound to PLP, takes an asymmetric structure. Structural evidence that alanine racemase from a D-cycloserine-producing microorganism exhibits resistance to its own product.,Noda M, Matoba Y, Kumagai T, Sugiyama M J Biol Chem. 2004 Oct 29;279(44):46153-61. Epub 2004 Aug 9. PMID:15302886 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Alanine racemase 3D structures

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