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1v0s
From Proteopedia
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| - | [[Image:1v0s.gif|left|200px]]<br /> | ||
| - | <applet load="1v0s" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1v0s, resolution 1.75Å" /> | ||
| - | '''UNINHIBITED FORM OF PHOSPHOLIPASE D FROM STREPTOMYCES SP. STRAIN PMF'''<br /> | ||
| - | == | + | ==Uninhibited form of Phospholipase D from Streptomyces sp. strain PMF== |
| - | Almost all enzyme-catalysed phosphohydrolytic or phosphoryl transfer | + | <StructureSection load='1v0s' size='340' side='right'caption='[[1v0s]], [[Resolution|resolution]] 1.75Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1v0s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._PMF Streptomyces sp. PMF]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V0S FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v0s OCA], [https://pdbe.org/1v0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v0s RCSB], [https://www.ebi.ac.uk/pdbsum/1v0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v0s ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/P84147_STRSM P84147_STRSM] | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v0/1v0s_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1v0s ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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 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<ref>PMID:15165852</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1v0s" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Phospholipase D 3D structures|Phospholipase D 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces sp. PMF]] | ||
| + | [[Category: Hough E]] | ||
| + | [[Category: Leiros I]] | ||
| + | [[Category: McSweeney S]] | ||
Current revision
Uninhibited form of Phospholipase D from Streptomyces sp. strain PMF
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