1h0r | pdb_00001h0r

Type II Dehydroquinase from Mycobacterium tuberculosis complexed with 2,3-anhydro-quinic acid

spinqualitylabelsall models 1h0r, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1h0r is a 1 chain structure with sequence from Myctu. The April 2010 RCSB PDB Molecule of the Month feature on Concanavalin A and Circular Permutation by David Goodsell is 10.2210/rcsb_pdb/mom_2010_4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, FA1, GOL, PO4 Related: 1h05, 1h0s, 2dhq Activity: 3-dehydroquinate dehydratase, with EC number 4.2.1.10 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AROQ_MYCTU] Catalyzes a trans-dehydration via an enolate intermediate (By similarity).[HAMAP-Rule:MF_00169] 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 The structures of enzymes catalyzing the reactions in central metabolic pathways are generally well conserved as are their catalytic mechanisms. The two types of 3-dehydroquinate dehydratase (DHQase) are therefore most unusual since they are unrelated at the sequence level and they utilize completely different mechanisms to catalyze the same overall reaction. The type I enzymes catalyze a cis-dehydration of 3-dehydroquinate via a covalent imine intermediate, while the type II enzymes catalyze a trans-dehydration via an enolate intermediate. Here we report the three-dimensional structures of a representative member of each type of biosynthetic DHQase. Both enzymes function as part of the shikimate pathway, which is essential in microorganisms and plants for the biosynthesis of aromatic compounds including folate, ubiquinone and the aromatic amino acids. An explanation for the presence of two different enzymes catalyzing the same reaction is presented. The absence of the shikimate pathway in animals makes it an attractive target for antimicrobial agents. The availability of these two structures opens the way for the design of highly specific enzyme inhibitors with potential importance as selective therapeutic agents. The two types of 3-dehydroquinase have distinct structures but catalyze the same overall reaction.,Gourley DG, Shrive AK, Polikarpov I, Krell T, Coggins JR, Hawkins AR, Isaacs NW, Sawyer L Nat Struct Biol. 1999 Jun;6(6):521-5. PMID:10360352 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dehydroquinase 3D structures

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