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1v0v

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{{STRUCTURE_1v0v| PDB=1v0v | SCENE= }}
{{STRUCTURE_1v0v| PDB=1v0v | SCENE= }}
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'''PHOSPHOLIPASE D FROM STREPTOMYCES SP. STRAIN PMF SOAKED WITH THE SUBSTRATE DIBUTYRYLPHOSPHATIDYLCHOLINE.'''
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===PHOSPHOLIPASE D FROM STREPTOMYCES SP. STRAIN PMF SOAKED WITH THE SUBSTRATE DIBUTYRYLPHOSPHATIDYLCHOLINE.===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15165852 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15165852}}
==About this Structure==
==About this Structure==
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[[Category: Phospholipase d]]
[[Category: Phospholipase d]]
[[Category: Substrate soak]]
[[Category: Substrate soak]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:56:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:14:41 2008''

Revision as of 02:14, 29 July 2008

Image:1v0v.png

Template:STRUCTURE 1v0v

PHOSPHOLIPASE D FROM STREPTOMYCES SP. STRAIN PMF SOAKED WITH THE SUBSTRATE DIBUTYRYLPHOSPHATIDYLCHOLINE.

Template:ABSTRACT PUBMED 15165852

About this Structure

1V0V is a Single protein structure of sequence from Streptomyces sp.. 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 Tue Jul 29 05:14:41 2008

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