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Structure paper

TitleBiosynthesis of pteridines. Reaction mechanism of GTP cyclohydrolase I.
Journal, issue, pagesJ. Mol. Biol., Vol. 326, Page 503-516, Year 2003
Publish dateMar 27, 1998 (structure data deposition date)
AuthorsRebelo, J. / Auerbach, G. / Bader, G. / Bracher, A. / Nar, H. / Hosl, C. / Schramek, N. / Kaiser, J. / Bacher, A. / Huber, R. / Fischer, M.
External linksJ. Mol. Biol. / PubMed:12559918
MethodsX-ray diffraction
Resolution2.1 - 3.2 Å
Structure data

PDB-1a8r:
GTP CYCLOHYDROLASE I (H112S MUTANT) IN COMPLEX WITH GTP
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1n3r:
Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-1n3s:
Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I
Method: X-RAY DIFFRACTION / Resolution: 2.55 Å

PDB-1n3t:
Biosynthesis of pteridins. Reaction mechanism of GTP cyclohydrolase I
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / GTP / PURINE HYDROLYSIS / PTERINE SYNTHESIS / Biosynthesis / folic acid / GTP cyclohydrolase I / tetrahydropterin / pteridines

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