1GTP

GTP CYCLOHYDROLASE I

Summary for 1GTP

Entry DOI	10.2210/pdb1gtp/pdb
Descriptor	GTP CYCLOHYDROLASE I, SULFATE ION (3 entities in total)
Functional Keywords	gtp, purine hydrolysis, pterine synthesis, hydrolase
Biological source	Escherichia coli
Total number of polymer chains	20
Total formula weight	496590.28
Authors	Nar, H.,Huber, R.,Meining, W.,Bacher, A. (deposition date: 1995-09-16, release date: 1996-11-08, Last modification date: 2024-10-23)
Primary citation	Nar, H.,Huber, R.,Meining, W.,Schmid, C.,Weinkauf, S.,Bacher, A. Atomic structure of GTP cyclohydrolase I. Structure, 3:459-466, 1995 Cited by PubMed Abstract: Tetrahydrobiopterin serves as the cofactor for enzymes involved in neurotransmitter biosynthesis and as regulatory factor in immune cell proliferation and the biosynthesis of melanin. The biosynthetic pathway to tetrahydrobiopterin consists of three steps starting from GTP. The initial reaction is catalyzed by GTP cyclohdrolase I (GTP-CH-I) and involves the chemically complex transformation of the purine into the pterin ring system. PubMed: 7663943 DOI: 10.1016/S0969-2126(01)00179-4 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (3 Å)

Structure validation