2gqn

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{{STRUCTURE_2gqn| PDB=2gqn | SCENE= }}
{{STRUCTURE_2gqn| PDB=2gqn | SCENE= }}
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'''Cystathionine Beta-Lyase (CBL) from Escherichia Coli in complex with N-Hydrazinocarbonylmethyl-2-Nitro-Benzamide'''
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===Cystathionine Beta-Lyase (CBL) from Escherichia Coli in complex with N-Hydrazinocarbonylmethyl-2-Nitro-Benzamide===
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==Overview==
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The biosynthesis of methionine is an attractive antibiotic target given its importance in protein and DNA metabolism and its absence in mammals. We have performed a high-throughput screen of the methionine biosynthesis enzyme cystathionine beta-lyase (CBL) against a library of 50 000 small molecules and have identified several compounds that inhibit CBL enzyme activity in vitro. These hit molecules were of two classes: those that blocked CBL activity with mixed steady-state inhibition and those that covalently interacted with the enzyme at the active site pyridoxal phosphate cofactor with slow-binding inhibition kinetics. We determined the crystal structure of one of the slow-binding inhibitors in complex with CBL and used this structure as a guide in the synthesis of a small, focused library of analogues, some of which had improved enzyme inhibition properties. These studies provide the first lead molecules for antimicrobial agents that target cystathionine beta-lyase in methionine biosynthesis.
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{{ABSTRACT_PUBMED_17300162}}
==About this Structure==
==About this Structure==
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[[Category: Plp cofactor covalently bount to blp inhibitor]]
[[Category: Plp cofactor covalently bount to blp inhibitor]]
[[Category: Protein-inhibitor complex]]
[[Category: Protein-inhibitor complex]]
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Revision as of 00:45, 28 July 2008

Image:2gqn.png

Template:STRUCTURE 2gqn

Cystathionine Beta-Lyase (CBL) from Escherichia Coli in complex with N-Hydrazinocarbonylmethyl-2-Nitro-Benzamide

Template:ABSTRACT PUBMED 17300162

About this Structure

2GQN is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Inhibitors of bacterial cystathionine beta-lyase: leads for new antimicrobial agents and probes of enzyme structure and function., Ejim LJ, Blanchard JE, Koteva KP, Sumerfield R, Elowe NH, Chechetto JD, Brown ED, Junop MS, Wright GD, J Med Chem. 2007 Feb 22;50(4):755-64. PMID:17300162

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