2fqo: Difference between revisions

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[[Image:2fqo.gif|left|200px]]
{{Seed}}
[[Image:2fqo.png|left|200px]]


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{{STRUCTURE_2fqo|  PDB=2fqo  |  SCENE=  }}  
{{STRUCTURE_2fqo|  PDB=2fqo  |  SCENE=  }}  


'''Crystal structure of B. subtilis LuxS in complex with (2S)-2-Amino-4-[(2R,3R)-2,3-dihydroxy-3-N- hydroxycarbamoyl-propylmercapto]butyric acid'''
===Crystal structure of B. subtilis LuxS in complex with (2S)-2-Amino-4-[(2R,3R)-2,3-dihydroxy-3-N- hydroxycarbamoyl-propylmercapto]butyric acid===




==Overview==
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S-Ribosylhomocysteinase (LuxS) catalyzes the cleavage of the thioether linkage in S-ribosylhomocysteine (SRH) to produce homocysteine and 4,5-dihydroxy-2,3-pentanedione, the precursor of autoinducer 2. Inhibitors of LuxS should interfere with bacterial interspecies communication and potentially provide a novel class of antibacterial agents. LuxS utilizes a divalent metal ion as a Lewis acid during catalysis. In this work, a series of structural analogues of the substrate SRH and a 2-ketone intermediate were designed and synthesized. Kinetic studies indicate that the compounds act as reversible, competitive inhibitors against LuxS, with the most potent inhibitors having K(I) values in the submicromolar range. These represent the most potent LuxS inhibitors that have been reported to date. Cocrystal structures of LuxS bound with two of the inhibitors largely confirmed the design principles, i.e., the importance of both the homocysteine and ribose moieties in high-affinity binding to the LuxS active site.
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{{ABSTRACT_PUBMED_16686542}}


==About this Structure==
==About this Structure==
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[[Category: Lux]]
[[Category: Lux]]
[[Category: Quorum sensing]]
[[Category: Quorum sensing]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 04:12:20 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:21:12 2008''

Revision as of 03:21, 28 July 2008

File:2fqo.png

Template:STRUCTURE 2fqo

Crystal structure of B. subtilis LuxS in complex with (2S)-2-Amino-4-[(2R,3R)-2,3-dihydroxy-3-N- hydroxycarbamoyl-propylmercapto]butyric acid

Template:ABSTRACT PUBMED 16686542

About this Structure

2FQO is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Design and synthesis of substrate and intermediate analogue inhibitors of S-ribosylhomocysteinase., Shen G, Rajan R, Zhu J, Bell CE, Pei D, J Med Chem. 2006 May 18;49(10):3003-11. PMID:16686542

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