1FB1

CRYSTAL STRUCTURE OF HUMAN GTP CYCLOHYDROLASE I

Summary for 1FB1

• Entry DOI: 10.2210/pdb1fb1/pdb
• Descriptor: GTP CYCLOHYDROLASE I, ZINC ION, ISOPROPYL ALCOHOL (3 entities in total)
• Functional Keywords: hydrolase, allosteric enzyme, phosphorylation
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P30793
• Total number of polymer chains: 5
• Total formula weight: 111154.96

Authors

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. (deposition date: 2000-07-14, release date: 2000-12-08, Last modification date: 2024-02-07)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.1 Å)