Crystal structures of hint demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins

Charles Brenner, Preston Garrison, Jeffrey Gilmour, Daniel Peisach, Dagmar Ringe, Gregory A. Petsko, John M. Lowenstein

Research output: Contribution to journalArticlepeer-review

127 Scopus citations

Abstract

Histidine triad nucleotide-binding protein (HINT), a dimeric purine nucleotide-binding protein from rabbit heart, is a member of the HIT (histidine triad) superfamily which includes HINT homologues and FHIT (HIT protein encoded at the chromosome 3 fragile site) homologues. Crystal structures of HINT-nucleotide complexes demonstrate that the most conserved residues in the superfamily mediate nucleotide binding and that the HIT motif forms part of the phosphate binding loop. Galactose-1-phosphate uridylyltransferase, whose deficiency causes galactosemia, contains tandem HINT domains with the same fold and mode of nucleotide binding as HINT despite having no overall sequence similarity. Features of FHIT, a diadenosine polyphosphate hydrolase and candidate tumour suppressor, are predicted from HINT-nucleotide structures.

Original languageEnglish (US)
Pages (from-to)231-238
Number of pages8
JournalNature Structural Biology
Volume4
Issue number3
DOIs
StatePublished - Mar 1997

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

Fingerprint

Dive into the research topics of 'Crystal structures of hint demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins'. Together they form a unique fingerprint.

Cite this