4fit: Difference between revisions

Revision as of 20:13, 21 February 2008

FHIT-APO

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

4FIT is a Single protein structure of sequence from Homo sapiens. 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

Page seeded by OCA on Thu Feb 21 19:13:17 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 4: / Line 4: @@
 ==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 identified through genomics.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Hendrickson, W.A.]]
+[[Category: Hendrickson, W A.]]
-[[Category: Klein, M.G.]]
+[[Category: Klein, M G.]]
-[[Category: Lima, C.D.]]
+[[Category: Lima, C D.]]
 [[Category: fhit]]
 [[Category: fragile histidine triad protein]]
@@ Line 26: / Line 26: @@
 [[Category: putative tumor suppressor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:52:52 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:13:17 2008''