1v2d | pdb_00001v2d

Crystal Structure of T.th HB8 Glutamine Aminotransferase

spinqualitylabelsall models 1v2d, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1v2d is a 1 chain structure with sequence from "flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PLP Related: 1v2e, 1v2f Gene: HB8 ("Flavobacterium thermophilum" Yoshida and Oshima 1971) Activity: Glutamine--pyruvate transaminase, with EC number 2.6.1.15 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, TOPSAN 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 following three-dimensional structures of three forms of glutamine:phenylpyruvate aminotransferase from Thermus thermophilus HB8 have been determined and represent the first x-ray analysis of the enzyme: the unliganded pyridoxal 5'-phosphate form at 1.9 A resolution and two complexes with 3-phenylpropionate and alpha-keto-gamma-methylthiobutyrate at 2.35 and 2.6 A resolution, respectively. The enzyme shows high activity toward phenylalanine, tyrosine, tryptophan, kynurenine, methionine, and glutamine. The enzyme is a homodimer, and each subunit is divided into an N-terminal arm and small and large domains. Based on its folding, the enzyme belongs to fold type I, aminotransferase subclass Ib. The subclass I aminotransferases whose structures have so far been determined exhibit a large movement of the small domain region upon binding of a substrate. Similarly, the glutamine:phenylpyruvate aminotransferase undergoes a large movement in part of the small domain to close the active site. The active-site pocket has a shape and size suitable to enclose the side chain of an aromatic amino acid or that of methionine. The inner side of the pocket is mostly hydrophobic, but also has polar sites. The kynurenine complex generated by computer modeling fits the pocket of the enzyme and its hydrophilic groups interact with the polar sites of the pocket. Crystal structures of glutamine:phenylpyruvate aminotransferase from Thermus thermophilus HB8: induced fit and substrate recognition.,Goto M, Omi R, Miyahara I, Hosono A, Mizuguchi H, Hayashi H, Kagamiyama H, Hirotsu K J Biol Chem. 2004 Apr 16;279(16):16518-25. Epub 2004 Feb 3. PMID:14761974 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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