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

doi:10.1038/nsb0397-231

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

Journal article

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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 and John M Lowenstein

Nature structural biology, Vol.4(3), pp.231-238

03/1997

DOI: https://doi.org/10.1038/nsb0397-231

PMCID: PMC2571075

PMID: 9164465

Abstract

protein

crystal structures

HINT

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 homologs and FHIT homologs. 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 no overall sequence similarity. Features of FHIT, a diadenosine polyphosphate hydrolase and candidate tumor suppressor, are predicted from HINT-nucleotide structures.

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Title: Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins
Creators: Charles Brenner - Departments of Biochemistry and Chemistry and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254, USA
Preston Garrison - Department of Biochemistry, University of Texas Health Sciences Center, San Antonio, Texas 78284, USA
Jeffrey Gilmour - Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254, USA
Daniel Peisach - Departments of Biochemistry and Chemistry and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254, USA
Dagmar Ringe - Departments of Biochemistry and Chemistry and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254, USA
Gregory A Petsko - Departments of Biochemistry and Chemistry and Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254, USA
John M Lowenstein - Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254, USA
Publication Details: Nature structural biology, Vol.4(3), pp.231-238
Identifiers: 9923958357301921
Academic Unit: Rosenstiel Basic Medical Sciences Research Center; Department of Biochemistry; Interdepartmental Program in Neuroscience; Department of Chemistry
Language: English
Resource Type: Journal article

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

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