1v0s

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spinqualitylabelsall models 1v0s, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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, different time-steps. Both substrate and product-structures were, determined in order to identify the different reaction states and to, examine if the reaction actually terminated on formation of phosphatidic, acid (the true product of phospholipase D action) or could proceed even, further. The results presented support the theory that the phospholipase D, superfamily shares a common reaction mechanism, although different family, members have very different substrate preferences and perform different, catalytic reactions. Results also show that the reaction proceeds via a, phosphohistidine intermediate and provide unambiguous identification of a, catalytic water molecule, ideally positioned for apical attack on the, phosphorus and consistent with an associative in-line phosphoryl transfer, reaction. In one of the experiments an apparent five-coordinate phosphorus, transition state is observed.

About this Structure

1V0S is a Single protein structure of sequence from Streptomyces sp.. Active as Phospholipase D, with EC number 3.1.4.4 Known structural/functional Site: . 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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