Crystal structure of rat GTP cyclohydrolase I feedback regulatory protein, GFRP

J Mol Biol. 2001 Oct 5;312(5):1051-7. doi: 10.1006/jmbi.2001.5011.

Abstract

Tetrahydrobiopterin, the cofactor required for hydroxylation of aromatic amino acids regulates its own synthesis in mammals through feedback inhibition of GTP cyclohydrolase I. This mechanism is mediated by a regulatory subunit called GTP cyclohydrolase I feedback regulatory protein (GFRP). The 2.6 A resolution crystal structure of rat GFRP shows that the protein forms a pentamer. This indicates a model for the interaction of mammalian GTP cyclohydrolase I with its regulator, GFRP. Kinetic investigations of human GTP cyclohydrolase I in complex with rat and human GFRP showed similar regulatory effects of both GFRP proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Crystallography, X-Ray
  • Feedback
  • GTP Cyclohydrolase / antagonists & inhibitors*
  • GTP Cyclohydrolase / chemistry
  • GTP Cyclohydrolase / metabolism*
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Kinetics
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Structure, Quaternary
  • Proteins / chemistry*
  • Proteins / metabolism*
  • Rats
  • Sequence Alignment
  • Static Electricity

Substances

  • GCHFR protein, human
  • Gchfr protein, rat
  • Intracellular Signaling Peptides and Proteins
  • Proteins
  • GTP Cyclohydrolase

Associated data

  • PDB/1JG5