5FIT

FHIT-SUBSTRATE ANALOG

Summary for 5FIT

• Entry DOI: 10.2210/pdb5fit/pdb
• Descriptor: FRAGILE HISTIDINE TRIAD PROTEIN, PHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER (3 entities in total)
• Functional Keywords: hydrolase, fragile histidine triad protein, fhit, putative tumor suppressor, hit protein family, histidine triad protein family, nucleotidyl hydrolase, nucleotidyl transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P49789
• Total number of polymer chains: 1
• Total formula weight: 17405.22

Authors

Lima, C.D.,Klein, M.G.,Hendrickson, W.A. (deposition date: 1997-09-25, release date: 1998-03-25, Last modification date: 2024-11-20)

Primary citation

Lima, C.D.,Klein, M.G.,Hendrickson, W.A.
Structure-based analysis of catalysis and substrate definition in the HIT protein family.
Science, 278:286-290, 1997

PubMed 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.

PubMed: 9323207
DOI: 10.1126/science.278.5336.286

Experimental method

X-RAY DIFFRACTION (2.3 Å)