FHIT-TRANSITION STATE ANALOG

File:6fit.gif


6fit, resolution 2.6Å

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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 AMW as ligand. Active as Bis(5'-adenosyl)-triphosphatase, with EC number 3.6.1.29 Structure known Active Sites: AVE and HNE. 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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