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1v0s
From Proteopedia
(New page: 200px<br /> <applet load="1v0s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v0s, resolution 1.75Å" /> '''UNINHIBITED FORM OF...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1V0S is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.4 3.1.4.4]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V0S OCA]]. | + | 1V0S is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]]. 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]]. Structure known Active Site: 1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V0S OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15165852 15165852] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15165852 15165852] | ||
| + | [[Category: Phospholipase D]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces sp.]] | [[Category: Streptomyces sp.]] | ||
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[[Category: uninhibited]] | [[Category: uninhibited]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:30:04 2007'' |
Revision as of 11:25, 30 October 2007
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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, ... [(full description)]
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]. 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
Page seeded by OCA on Tue Oct 30 13:30:04 2007
