1kt9
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1kt9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kt9, resolution 1.98Å" /> '''Crystal Structure of...)
Next diff →
Revision as of 17:43, 20 November 2007
|
Crystal Structure of C. elegans Ap4A Hydrolase
Overview
The crystal structure of C. elegans Ap(4)A hydrolase has been determined, for the free enzyme and a binary complex at 2.0 A and 1.8 A, respectively., Ap(4)A hydrolase has a key role in regulating the intracellular Ap(4)A, levels and hence potentially the cellular response to metabolic stress, and/or differentiation and apoptosis via the Ap(3)A/Ap(4)A ratio. The, structures reveal that the enzyme has the mixed alpha/beta fold of the, Nudix family and also show how the enzyme binds and locates its substrate, with respect to the catalytic machinery of the Nudix motif. These results, suggest how the enzyme can catalyze the hydrolysis of a range of related, dinucleoside tetraphosphate, but not triphosphate, compounds through, precise orientation of key elements of the substrate.
About this Structure
1KT9 is a Single protein structure of sequence from Caenorhabditis elegans. Active as Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical), with EC number 3.6.1.17 Full crystallographic information is available from OCA.
Reference
The crystal structure of diadenosine tetraphosphate hydrolase from Caenorhabditis elegans in free and binary complex forms., Bailey S, Sedelnikova SE, Blackburn GM, Abdelghany HM, Baker PJ, McLennan AG, Rafferty JB, Structure. 2002 Apr;10(4):589-600. PMID:11937063
Page seeded by OCA on Tue Nov 20 19:50:33 2007
