2fq6
From Proteopedia
(New page: 200px<br /><applet load="2fq6" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fq6, resolution 1.78Å" /> '''Cystathionine beta-l...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2fq6.jpg|left|200px]]<br /><applet load="2fq6" size=" | + | [[Image:2fq6.jpg|left|200px]]<br /><applet load="2fq6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fq6, resolution 1.78Å" /> | caption="2fq6, resolution 1.78Å" /> | ||
'''Cystathionine beta-lyase (cbl) from escherichia coli in complex with n-hydrazinocarbonylmethyl-2-trifluoromethyl-benzamide'''<br /> | '''Cystathionine beta-lyase (cbl) from escherichia coli in complex with n-hydrazinocarbonylmethyl-2-trifluoromethyl-benzamide'''<br /> | ||
| Line 7: | Line 7: | ||
==About this Structure== | ==About this Structure== | ||
| - | 2FQ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with P3F as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cystathionine_beta-lyase Cystathionine beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.8 4.4.1.8] Full crystallographic information is available from [http:// | + | 2FQ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=P3F:'>P3F</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cystathionine_beta-lyase Cystathionine beta-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.8 4.4.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FQ6 OCA]. |
==Reference== | ==Reference== | ||
| Line 19: | Line 19: | ||
[[Category: protein-inhibitor complex]] | [[Category: protein-inhibitor complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:23:53 2008'' |
Revision as of 13:23, 23 January 2008
|
Cystathionine beta-lyase (cbl) from escherichia coli in complex with n-hydrazinocarbonylmethyl-2-trifluoromethyl-benzamide
Overview
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.
About this Structure
2FQ6 is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Cystathionine beta-lyase, with EC number 4.4.1.8 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
Page seeded by OCA on Wed Jan 23 15:23:53 2008
