1v2f
From Proteopedia
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Crystal Structure of T.th HB8 Glutamine Aminotransferase complex with 3-phenylpropionate
Overview
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.
About this Structure
1V2F is a Single protein structure of sequence from Thermus thermophilus with PLP and HCI as ligands. Active as Glutamine--pyruvate transaminase, with EC number 2.6.1.15 Full crystallographic information is available from OCA.
Reference
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
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