2or2

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[[Image:2or2.gif|left|200px]]<br /><applet load="2or2" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2or2, resolution 1.840&Aring;" />
 
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'''Structure of the W47A/W242A Mutant of Bacterial Phosphatidylinositol-Specific Phospholipase C'''<br />
 
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==Overview==
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==Structure of the W47A/W242A Mutant of Bacterial Phosphatidylinositol-Specific Phospholipase C==
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The crystal structure of the W47/242A mutant of, phosphatidylinositol-specific phospholipase C (PI-PLC) from Bacillus, thuringiensis has been solved to 1.8 A resolution. The W47/242A mutant is, an interfacially-challenged enzyme, and it has been proposed that one or, both tryptophan side chains serve as membrane interfacial anchors (Feng et, al. (2002) J. Biol. Chem. 277, 19867-75). The crystal structure supports, this hypothesis. Relative to the crystal structure of the closely-related, (97% identity) wild-type PI-PLC from B. cereus, significant conformational, differences occur at the membrane-binding interfacial region rather than, the active site. The TrpAla mutations not only remove the, membrane-partitioning aromatic side chains but also perturb the, conformations of the so-called helix B and rim loop regions, both of which, are implicated in interfacial binding. The crystal structure also reveals, a homodimer, the first such observation for a bacterial PI-PLC, with, pseudo 2-fold symmetry. The symmetric dimer interface is stabilized by, hydrophobic and hydrogen-bonding interactions, contributed primarily by a, central swath of aromatic residues arranged in a quasi-herringbone, pattern. Evidence that interfacially-active wild-type PI-PLC enzymes may, dimerize in the presence of phosphatidylcholine vesicles is provided by, fluorescence quenching of PI-PLC mutants with pyrene-labeled cysteine, residues. The combined data suggest that wild-type PI-PLC can form similar, homodimers, anchored to the interface by the tryptophan and neighboring, membrane-partitioning residues.
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<StructureSection load='2or2' size='340' side='right'caption='[[2or2]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2or2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OR2 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2or2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2or2 OCA], [https://pdbe.org/2or2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2or2 RCSB], [https://www.ebi.ac.uk/pdbsum/2or2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2or2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PLC_BACTU PLC_BACTU] Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/or/2or2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2or2 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2OR2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Active as [http://en.wikipedia.org/wiki/Phosphatidylinositol_diacylglycerol-lyase Phosphatidylinositol diacylglycerol-lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.13 4.6.1.13] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OR2 OCA].
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*[[Phospholipase C|Phospholipase C]]
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__TOC__
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==Reference==
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</StructureSection>
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Dimer structure of an interfacially impaired phosphatidylinositol-specific phospholipase C., Shao C, Shi X, Wehbi H, Zambonelli C, Head JF, Seaton BA, Roberts MF, J Biol Chem. 2007 Jan 9;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17213187 17213187]
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[[Category: Bacillus thuringiensis]]
[[Category: Bacillus thuringiensis]]
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[[Category: Phosphatidylinositol diacylglycerol-lyase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Head JF]]
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[[Category: Head, J.F.]]
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[[Category: Roberts MF]]
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[[Category: Roberts, M.F.]]
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[[Category: Seaton BA]]
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[[Category: Seaton, B.A.]]
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[[Category: Shao C]]
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[[Category: Shao, C.]]
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[[Category: Shi X]]
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[[Category: Shi, X.]]
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[[Category: Wehbi H]]
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[[Category: Wehbi, H.]]
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[[Category: Zambonelli C]]
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[[Category: Zambonelli, C.]]
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[[Category: dimer]]
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[[Category: interfacially impaired]]
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[[Category: membrane binding]]
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[[Category: phosphatidylinositol-specific phospholipase c]]
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[[Category: pi-plc]]
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[[Category: tim barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:04:26 2008''
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Current revision

Structure of the W47A/W242A Mutant of Bacterial Phosphatidylinositol-Specific Phospholipase C

PDB ID 2or2

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