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1vft

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{{STRUCTURE_1vft| PDB=1vft | SCENE= }}
{{STRUCTURE_1vft| PDB=1vft | SCENE= }}
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'''Crystal structure of L-cycloserine-bound form of alanine racemase from D-cycloserine-producing Streptomyces lavendulae'''
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===Crystal structure of L-cycloserine-bound form of alanine racemase from D-cycloserine-producing Streptomyces lavendulae===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_15302886}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/15302886 15302886]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15302886 15302886]
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Self-protection mechanism in D-cycloserine-producing Streptomyces lavendulae. Gene cloning, characterization, and kinetics of its alanine racemase and D-alanyl-D-alanine ligase, which are target enzymes of D-cycloserine., Noda M, Kawahara Y, Ichikawa A, Matoba Y, Matsuo H, Lee DG, Kumagai T, Sugiyama M, J Biol Chem. 2004 Oct 29;279(44):46143-52. Epub 2004 Aug 9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15302885 15302885]
[[Category: Alanine racemase]]
[[Category: Alanine racemase]]
[[Category: Kumagai, T.]]
[[Category: Kumagai, T.]]
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[[Category: Greek-key motief]]
[[Category: Greek-key motief]]
[[Category: Tim-barrel]]
[[Category: Tim-barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:29:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:51:14 2008''

Revision as of 20:51, 28 July 2008

Image:1vft.png

Template:STRUCTURE 1vft

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

Template:ABSTRACT PUBMED 15302886

About this Structure

Full crystallographic information is available from OCA.

Reference

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

Self-protection mechanism in D-cycloserine-producing Streptomyces lavendulae. Gene cloning, characterization, and kinetics of its alanine racemase and D-alanyl-D-alanine ligase, which are target enzymes of D-cycloserine., Noda M, Kawahara Y, Ichikawa A, Matoba Y, Matsuo H, Lee DG, Kumagai T, Sugiyama M, J Biol Chem. 2004 Oct 29;279(44):46143-52. Epub 2004 Aug 9. PMID:15302885

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