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Structure-based analysis of catalysis and substrate definition in the HIT protein family.

Lima CD, Klein MG, Hendrickson WA
Science 278 286-90 (1997)
Related entries: 1av5, 1kpe, 4fit, 5fit, 6fit

Cited: 161 times
EuropePMC logo PMID: 9323207

Abstract

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.

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  1. Three-Dimensional Structure of Human Protein Kinase C Interacting Protein 1, a Member of the Hit Family of Proteins. Lima CD, Klein MG, Weinstein IB, Hendrickson WA Proc. Natl. Acad. Sci. U.S.A. 93 5357- (1996)

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