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

spinqualitylabelsall models 2fqo, resolution 1.87Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2fqo is a 1 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.87Å Ligands: CO, HYI, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function LUXS_BACSU Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).[HAMAP-Rule:MF_00091] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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