1FB1

CRYSTAL STRUCTURE OF HUMAN GTP CYCLOHYDROLASE I

1FB1 の概要

• エントリーDOI: 10.2210/pdb1fb1/pdb
• 分子名称: GTP CYCLOHYDROLASE I, ZINC ION, ISOPROPYL ALCOHOL (3 entities in total)
• 機能のキーワード: hydrolase, allosteric enzyme, phosphorylation
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P30793
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 111154.96

構造登録者

Auerbach, G.,Herrmann, A.,Bracher, A.,Bader, G.,Gutlich, M.,Fischer, M.,Neukamm, M.,Nar, H.,Garrido-Franco, M.,Richardson, J.,Huber, R.,Bacher, A. (登録日: 2000-07-14, 公開日: 2000-12-08, 最終更新日: 2024-02-07)

主引用文献

Auerbach, G.,Herrmann, A.,Bracher, A.,Bader, G.,Gutlich, M.,Fischer, M.,Neukamm, M.,Garrido-Franco, M.,Richardson, J.,Nar, H.,Huber, R.,Bacher, A.
Zinc plays a key role in human and bacterial GTP cyclohydrolase I.
Proc.Natl.Acad.Sci.USA, 97:13567-13572, 2000

PubMed Abstract: The crystal structure of recombinant human GTP cyclohydrolase I was solved by Patterson search methods by using the coordinates of the Escherichia coli enzyme as a model. The human as well as bacterial enzyme were shown to contain an essential zinc ion coordinated to a His side chain and two thiol groups in each active site of the homodecameric enzymes that had escaped detection during earlier studies of the E. coli enzyme. The zinc ion is proposed to generate a hydroxyl nucleophile for attack of imidazole ring carbon atom eight of the substrate, GTP. It may also be involved in the hydrolytic release of formate from the intermediate, 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-triphosphate, and in the consecutive Amadori rearrangement of the ribosyl moiety.

PubMed: 11087827
DOI: 10.1073/pnas.240463497

実験手法

X-RAY DIFFRACTION (3.1 Å)