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1d7u

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[[Image:1d7u.jpg|left|200px]]
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{{STRUCTURE_1d7u| PDB=1d7u | SCENE= }}
{{STRUCTURE_1d7u| PDB=1d7u | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE COMPLEX OF 2,2-DIALKYLGLYCINE DECARBOXYLASE WITH LCS'''
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===CRYSTAL STRUCTURE OF THE COMPLEX OF 2,2-DIALKYLGLYCINE DECARBOXYLASE WITH LCS===
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==Overview==
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The crystal structures of four inhibitor complexes of dialkylglycine decarboxylase are reported. The enzyme does not undergo a domain closure, as does aspartate aminotransferase, upon inhibitor binding. Two active-site conformations have been observed in previous structures that differ in alkali metal ion content, and two active-site conformations have been shown to coexist in solution when a single type of metal ion is present. There is no indication of coexisting conformers in the structures reported here or in the previously reported structures, and the observed conformation is that expected based on the presence of potassium in the enzyme. Thus, although two active-site conformations coexist in solution, a single conformation, corresponding to the more active enzyme, predominates in the crystal. The structure of 1-aminocyclopropane-1-carboxylate bound in the active site shows the aldimine double bond to the pyridoxal phosphate cofactor to be fully out of the plane of the coenzyme ring, whereas the Calpha-CO2(-) bond lies close to it. This provides an explanation for the observed lack of decarboxylation reactivity with this amino acid. The carboxylate groups of both 1-aminocyclopropane-1-carboxylate and 5'-phosphopyridoxyl-2-methylalanine interact with Ser215 and Arg406 as previously proposed. This demonstrates structurally that alternative binding modes, which constitute substrate inhibition, occur in the decarboxylation half-reaction. The structures of d and l-cycloserine bound to the active-site show that the l-isomer is deprotonated at C(alpha), presumably by Lys272, while the d-isomer is not. This difference explains the approximately 3000-fold greater potency of the l versus the d-isomer as a competitive inhibitor of dialkylglycine decarboxylase.
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(as it appears on PubMed at http://www.pubmed.gov), where 10556038 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10556038}}
==About this Structure==
==About this Structure==
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[[Category: Decarboxylation inhibitor]]
[[Category: Decarboxylation inhibitor]]
[[Category: Enzyme complex]]
[[Category: Enzyme complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:32:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:38:42 2008''

Revision as of 19:38, 30 June 2008

Image:1d7u.png

Template:STRUCTURE 1d7u

CRYSTAL STRUCTURE OF THE COMPLEX OF 2,2-DIALKYLGLYCINE DECARBOXYLASE WITH LCS

Template:ABSTRACT PUBMED 10556038

About this Structure

1D7U is a Single protein structure of sequence from Burkholderia cepacia. Full crystallographic information is available from OCA.

Reference

Crystal structures of dialkylglycine decarboxylase inhibitor complexes., Malashkevich VN, Strop P, Keller JW, Jansonius JN, Toney MD, J Mol Biol. 1999 Nov 19;294(1):193-200. PMID:10556038

Page seeded by OCA on Mon Jun 30 22:38:42 2008

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