6fit
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FHIT-TRANSITION STATE ANALOG
OverviewOverview
The histidine triad (HIT) protein family is among the most ubiquitous and highly conserved in nature, but a biological activity has not yet been identified for any member of the HIT family. Fragile histidine triad protein (FHIT) and protein kinase C interacting protein (PKCI) were used in a structure-based approach to elucidate characteristics of in vivo ligands and reactions. Crystallographic structures of apo, substrate analog, pentacovalent transition-state analog, and product states of both enzymes reveal a catalytic mechanism and define substrate characteristics required for catalysis, thus unifying the HIT family as nucleotidyl hydrolases, transferases, or both. The approach described here may be useful in identifying structure-function relations between protein families identified through genomics.
About this StructureAbout this Structure
6FIT is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Bis(5'-adenosyl)-triphosphatase, with EC number 3.6.1.29 Known structural/functional Sites: and . Full crystallographic information is available from OCA.
ReferenceReference
Structure-based analysis of catalysis and substrate definition in the HIT protein family., Lima CD, Klein MG, Hendrickson WA, Science. 1997 Oct 10;278(5336):286-90. PMID:9323207
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