1v0s
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1v0s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v0s, resolution 1.75Å" /> '''UNINHIBITED FORM OF...)
Next diff →
Revision as of 18:36, 29 October 2007
|
UNINHIBITED FORM OF PHOSPHOLIPASE D FROM STREPTOMYCES SP. STRAIN PMF
Overview
Almost all enzyme-catalysed phosphohydrolytic or phosphoryl transfer, reactions proceed through a five-coordinated phosphorus transition state., This is also true for the phospholipase D superfamily of enzymes, where, the active site usually is made up of two identical sequence repeats of an, HKD motif, positioned around an approximate 2-fold axis, where the, histidine and lysine residues are essential for catalysis. An almost, complete reaction pathway has been elucidated by a series of experiments, where crystals of phospholipase D from Streptomyces sp. strain PMF, (PLD(PMF)) were soaked for different times with (i) a soluble poor, short-chained phospholipid substrate and (ii) with a product. The various, crystal structures were determined to a resolution of 1.35-1.75 A for the, ... [(full description)]
About this Structure
1V0S is a [Single protein] structure of sequence from [Streptomyces sp.]. Active as [[1]], with EC number [3.1.4.4]. Full crystallographic information is available from [OCA].
Reference
The reaction mechanism of phospholipase D from Streptomyces sp. strain PMF. Snapshots along the reaction pathway reveal a pentacoordinate reaction intermediate and an unexpected final product., Leiros I, McSweeney S, Hough E, J Mol Biol. 2004 Jun 11;339(4):805-20. PMID:15165852
Page seeded by OCA on Mon Oct 29 20:41:23 2007
