4cno | pdb_00004cno

Structure of the Salmonella typhi Type I dehydroquinase inhibited by a 3-dehydroquinic acid derivative

spinqualitylabelsall models 4cno, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4cno is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 9PY Related: 4cnn, 4cnp Activity: 3-dehydroquinate dehydratase, with EC number 4.2.1.10 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Structural, biochemical and computational studies to study substrate binding and the role of the conserved residues of the DHQ1 (type I dehydroquinase) enzyme active site are reported in the present paper. The crystal structure of DHQ1 from Salmonella typhi in complex with (2R)-2-methyl-3-dehydroquinic acid, a substrate analogue, was solved at 1.5 A. The present study reveals a previously unknown key role for conserved Glu46, Phe145 and Met205 and Gln236, Pro234 and Ala233 residues, with the latter three being located in the flexible substrate-covering loop. Gln236 was shown to be responsible for the folding of this loop and for the dramatic reduction of its flexibility, which triggers active site closure. Glu46 was found to be key in bringing the substrate close to the lysine/histidine catalytic pocket to initiate catalysis. The present study could be useful in the rational design of inhibitors of this challenging and recognized target for the development of novel herbicides and antimicrobial agents. Insights into substrate binding and catalysis in bacterial type I dehydroquinase.,Maneiro M, Peon A, Lence E, Otero JM, Van Raaij MJ, Thompson P, Hawkins AR, Gonzalez-Bello C Biochem J. 2014 Sep 15;462(3):415-24. doi: 10.1042/BJ20140614. PMID:24957267 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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