1vfs

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1vfs.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1vfs.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1vfs| PDB=1vfs | SCENE= }}
{{STRUCTURE_1vfs| PDB=1vfs | SCENE= }}
-
'''Crystal structure of D-cycloserine-bound form of alanine racemase from D-cycloserine-producing Streptomyces lavendulae'''
+
===Crystal structure of D-cycloserine-bound form of alanine racemase from D-cycloserine-producing Streptomyces lavendulae===
-
==Overview==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15302886}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15302886 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15302886}}
==About this Structure==
==About this Structure==
Line 20: Line 24:
==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]
 +
 +
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.]]
Line 27: Line 33:
[[Category: Greek-key motief]]
[[Category: Greek-key motief]]
[[Category: Tim-barrel]]
[[Category: Tim-barrel]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:29:32 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:55:45 2008''

Revision as of 10:55, 28 July 2008

Image:1vfs.png

Template:STRUCTURE 1vfs

Crystal structure of D-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

Page seeded by OCA on Mon Jul 28 13:55:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1vfs"
Personal tools