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| - | [[Image:1v0s.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1v0s| PDB=1v0s | SCENE= }} | | {{STRUCTURE_1v0s| PDB=1v0s | SCENE= }} |
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| - | '''UNINHIBITED FORM OF PHOSPHOLIPASE D FROM STREPTOMYCES SP. STRAIN PMF'''
| + | ===UNINHIBITED FORM OF PHOSPHOLIPASE D FROM STREPTOMYCES SP. STRAIN PMF=== |
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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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15165852}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15165852 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15165852}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Phospholipase d]] | | [[Category: Phospholipase d]] |
| | [[Category: Uninhibited]] | | [[Category: Uninhibited]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:56:54 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:22:19 2008'' |
Revision as of 03:22, 28 July 2008
Template:STRUCTURE 1v0s
UNINHIBITED FORM OF PHOSPHOLIPASE D FROM STREPTOMYCES SP. STRAIN PMF
Template:ABSTRACT PUBMED 15165852
About this Structure
1V0S 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 Mon Jul 28 06:22:19 2008
