1UU0

Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima (Apo-form)

1UU0 の概要

• エントリーDOI: 10.2210/pdb1uu0/pdb
• 関連するPDBエントリー: 1H1C 1UU1 1UU2
• 分子名称: HISTIDINOL-PHOSPHATE AMINOTRANSFERASE, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: histidine biosynthesis, transferase, aminotransferase, pyridoxal phosphate
• 由来する生物種: THERMOTOGA MARITIMA
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 157783.66

構造登録者

Vega, M.C.,Fernandez, F.J.,Lehmann, F.,Wilmanns, M. (登録日: 2003-12-12, 公開日: 2004-05-13, 最終更新日: 2023-12-13)

主引用文献

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

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: 15007066
DOI: 10.1074/JBC.M400291200

実験手法

X-RAY DIFFRACTION (2.85 Å)