1v0t

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[[Image:1v0t.jpg|left|200px]]<br /><applet load="1v0t" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1v0t.jpg|left|200px]]
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caption="1v0t, resolution 1.53&Aring;" />
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'''PHOSPHOLIPASE D FROM STREPTOMYCES SP. STRAIN PMF SOAKED WITH THE PRODUCT GLYCEROPHOSPHATE'''<br />
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{{Structure
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|PDB= 1v0t |SIZE=350|CAPTION= <scene name='initialview01'>1v0t</scene>, resolution 1.53&Aring;
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|SITE= <scene name='pdbsite=CAT:Catalytic+Residues'>CAT</scene>
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|LIGAND= <scene name='pdbligand=PO3:PHOSPHITE ION'>PO3</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''PHOSPHOLIPASE D FROM STREPTOMYCES SP. STRAIN PMF SOAKED WITH THE PRODUCT GLYCEROPHOSPHATE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=PO3:'>PO3</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1V0T OCA].
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1V0T is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V0T OCA].
==Reference==
==Reference==
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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]
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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://www.ncbi.nlm.nih.gov/pubmed/15165852 15165852]
[[Category: Phospholipase D]]
[[Category: Phospholipase D]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: product soak]]
[[Category: product soak]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:30:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:39:26 2008''

Revision as of 12:39, 20 March 2008


PDB ID 1v0t

Drag the structure with the mouse to rotate
, resolution 1.53Å
Sites:
Ligands:
Activity: Phospholipase D, with EC number 3.1.4.4
Coordinates: save as pdb, mmCIF, xml



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.. 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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