1v0t
From Proteopedia
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| - | [[Image:1v0t. | + | [[Image:1v0t.jpg|left|200px]]<br /><applet load="1v0t" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1v0t" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1v0t, resolution 1.53Å" /> | caption="1v0t, resolution 1.53Å" /> | ||
'''PHOSPHOLIPASE D FROM STREPTOMYCES SP. STRAIN PMF SOAKED WITH THE PRODUCT GLYCEROPHOSPHATE'''<br /> | '''PHOSPHOLIPASE D FROM STREPTOMYCES SP. STRAIN PMF SOAKED WITH THE PRODUCT GLYCEROPHOSPHATE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1V0T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.] with PO3 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phospholipase_D Phospholipase D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.4 3.1.4.4] | + | 1V0T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.] with PO3 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phospholipase_D Phospholipase D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.4 3.1.4.4] Known structural/functional Site: <scene name='pdbsite=CAT:Catalytic Residues'>CAT</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V0T OCA]. |
==Reference== | ==Reference== | ||
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[[Category: product soak]] | [[Category: product soak]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:21:06 2007'' |
Revision as of 16:11, 18 December 2007
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PHOSPHOLIPASE D FROM STREPTOMYCES SP. STRAIN PMF SOAKED WITH THE PRODUCT GLYCEROPHOSPHATE
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
1V0T is a Single protein structure of sequence from Streptomyces sp. with PO3 as ligand. 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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