1fb1
From Proteopedia
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| , resolution 3.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | GTP cyclohydrolase I, with EC number 3.5.4.16 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HUMAN GTP CYCLOHYDROLASE I
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Dystonia-5, DOPA-responsive OMIM:[600225], Phenylketonuria, atypical, due to GCH1 deficiency OMIM:[600225]
About this Structure
1FB1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Zinc plays a key role in human and bacterial GTP cyclohydrolase I., 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, Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13567-72. PMID:11087827
Page seeded by OCA on Thu Mar 20 11:06:46 2008
