2fqo
From Proteopedia
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|PDB= 2fqo |SIZE=350|CAPTION= <scene name='initialview01'>2fqo</scene>, resolution 1.87Å | |PDB= 2fqo |SIZE=350|CAPTION= <scene name='initialview01'>2fqo</scene>, resolution 1.87Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, | + | |LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=HYI:(2S)-2-AMINO-4-[(2R,3R)-2,3-DIHYDROXY-3-N-HYDROXYCARBAMOYL-PROPYLMERCAPTO]BUTYRIC+ACID'>HYI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/S-ribosylhomocysteine_lyase S-ribosylhomocysteine lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.21 4.4.1.21] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/S-ribosylhomocysteine_lyase S-ribosylhomocysteine lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.21 4.4.1.21] </span> |
|GENE= luxS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= luxS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2fqt|2FQT]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fqo OCA], [http://www.ebi.ac.uk/pdbsum/2fqo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fqo RCSB]</span> | ||
}} | }} | ||
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[[Category: Shen, G.]] | [[Category: Shen, G.]] | ||
[[Category: Zhu, J.]] | [[Category: Zhu, J.]] | ||
| - | [[Category: CO]] | ||
| - | [[Category: HYI]] | ||
| - | [[Category: SO4]] | ||
[[Category: lux]] | [[Category: lux]] | ||
[[Category: quorum sensing]] | [[Category: quorum sensing]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:06:28 2008'' |
Revision as of 00:06, 31 March 2008
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| , resolution 1.87Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | luxS (Bacillus subtilis) | ||||||
| Activity: | S-ribosylhomocysteine lyase, with EC number 4.4.1.21 | ||||||
| Related: | 2FQT
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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.
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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