6RHN

HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (HINT) FROM RABBIT WITHOUT NUCLEOTIDE

Summary for 6RHN

• Entry DOI: 10.2210/pdb6rhn/pdb
• Descriptor: HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN (2 entities in total)
• Functional Keywords: nucleotide-binding protein
• Biological source: Oryctolagus cuniculus (rabbit)
• Cellular location: Cytoplasm: P80912
• Total number of polymer chains: 1
• Total formula weight: 12584.53

Authors

Brenner, C.,Garrison, P.,Gilmour, J.,Peisach, D.,Ringe, D.,Petsko, G.A.,Lowenstein, J.M. (deposition date: 1997-02-27, release date: 1997-06-16, Last modification date: 2024-05-22)

Primary citation

Brenner, C.,Garrison, P.,Gilmour, J.,Peisach, D.,Ringe, D.,Petsko, G.A.,Lowenstein, J.M.
Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins.
Nat.Struct.Biol., 4:231-238, 1997

PubMed 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.

PubMed: 9164465
DOI: 10.1038/nsb0397-231

Experimental method

X-RAY DIFFRACTION (2.15 Å)