1UU1
Complex of Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima (Apo-form)
Summary for 1UU1
| Entry DOI | 10.2210/pdb1uu1/pdb |
| Related | 1H1C 1UU0 1UU2 |
| Descriptor | HISTIDINOL-PHOSPHATE AMINOTRANSFERASE, 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE, PHOSPHORIC ACID MONO-[2-AMINO-3-(3H-IMIDAZOL-4-YL)-PROPYL]ESTER, ... (4 entities in total) |
| Functional Keywords | histidine biosynthesis, transferase, aminotransferase, pyridoxal phosphate |
| Biological source | THERMOTOGA MARITIMA |
| Total number of polymer chains | 4 |
| Total formula weight | 159281.08 |
| Authors | Vega, M.C.,Fernandez, F.J.,Lehman, F.,Wilmanns, M. (deposition date: 2003-12-12, release date: 2004-03-18, Last modification date: 2023-12-13) |
| Primary citation | Fernandez, F.J.,Vega, M.C.,Lehmann, F.,Sandmeier, E.,Gehring, H.,Christen, P.,Wilmanns, M. Structural Studies of the Catalytic Reaction Pathway of a Hyperthermophilic Histidinol-Phosphate Aminotransferase J.Biol.Chem., 279:21478-, 2004 Cited by PubMed Abstract: In histidine biosynthesis, histidinol-phosphate aminotransferase catalyzes the transfer of the amino group from glutamate to imidazole acetol-phosphate producing 2-oxoglutarate and histidinol phosphate. In some organisms such as the hyperthermophile Thermotoga maritima, specific tyrosine and aromatic amino acid transaminases have not been identified to date, suggesting an additional role for histidinol-phosphate aminotransferase in other transamination reactions generating aromatic amino acids. To gain insight into the specific function of this transaminase, we have determined its crystal structure in the absence of any ligand except phosphate, in the presence of covalently bound pyridoxal 5'-phosphate, of the coenzyme histidinol phosphate adduct, and of pyridoxamine 5'-phosphate. The enzyme accepts histidinol phosphate, tyrosine, tryptophan, and phenylalanine, but not histidine, as substrates. The structures provide a model of how these different substrates could be accommodated by histidinol-phosphate aminotransferase. Some of the structural features of the enzyme are more preserved between the T. maritima enzyme and a related threonine-phosphate decarboxylase from S. typhimurium than with histidinol-phosphate aminotransferases from different organisms. PubMed: 15007066DOI: 10.1074/JBC.M400291200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.38 Å) |
Structure validation
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