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==Overview==
==Overview==
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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9323207 (full description)]]
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 Structure==
==About this Structure==
5FIT is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with AP2 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Bis(5'-adenosyl)-triphosphatase Bis(5'-adenosyl)-triphosphatase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.29 3.6.1.29]]. Structure known Active Sites: AVE and HNE. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=5FIT OCA]].  
5FIT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with AP2 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Bis(5'-adenosyl)-triphosphatase Bis(5'-adenosyl)-triphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.29 3.6.1.29] Structure known Active Sites: AVE and HNE. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=5FIT OCA].  


==Reference==
==Reference==
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[[Category: putative tumor suppressor]]
[[Category: putative tumor suppressor]]


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Revision as of 16:30, 5 November 2007

File:5fit.gif


5fit, resolution 2.3Å

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FHIT-SUBSTRATE 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

5FIT is a Single protein structure of sequence from Homo sapiens with AP2 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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