1v0y
From Proteopedia
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Revision as of 14:13, 30 October 2007
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PHOSPHOLIPASE D FROM STREPTOMYCES SP. STRAIN PMF SOAKED WITH THE SUBSTRATE DIBUTYRYLPHOSPHATIDYLCHOLINE.
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
1V0Y is a [Single protein] structure of sequence from [Streptomyces sp.] with HI5 as [ligand]. Active as [Phospholipase D], with EC number [3.1.4.4]. Structure known Active Site: 1. 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
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