2or2: Difference between revisions

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New page: left|200px<br /><applet load="2or2" size="450" color="white" frame="true" align="right" spinBox="true" caption="2or2, resolution 1.840Å" /> '''Structure of the W4...
 
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[[Image:2or2.gif|left|200px]]<br /><applet load="2or2" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2or2, resolution 1.840&Aring;" />
'''Structure of the W47A/W242A Mutant of Bacterial Phosphatidylinositol-Specific Phospholipase C'''<br />


==Overview==
==Structure of the W47A/W242A Mutant of Bacterial Phosphatidylinositol-Specific Phospholipase C==
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.
<StructureSection load='2or2' size='340' side='right'caption='[[2or2]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PLC_BACTU PLC_BACTU] Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates.
== 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/or/2or2_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=2or2 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OR2 OCA].
*[[Phospholipase C|Phospholipase C]]
 
__TOC__
==Reference==
</StructureSection>
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]
[[Category: Bacillus thuringiensis]]
[[Category: Bacillus thuringiensis]]
[[Category: Phosphatidylinositol diacylglycerol-lyase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Head JF]]
[[Category: Head, J.F.]]
[[Category: Roberts MF]]
[[Category: Roberts, M.F.]]
[[Category: Seaton BA]]
[[Category: Seaton, B.A.]]
[[Category: Shao C]]
[[Category: Shao, C.]]
[[Category: Shi X]]
[[Category: Shi, X.]]
[[Category: Wehbi H]]
[[Category: Wehbi, H.]]
[[Category: Zambonelli C]]
[[Category: Zambonelli, C.]]
[[Category: dimer]]
[[Category: interfacially impaired]]
[[Category: membrane binding]]
[[Category: phosphatidylinositol-specific phospholipase c]]
[[Category: pi-plc]]
[[Category: tim barrel]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:15:52 2007''

Latest revision as of 09:05, 21 February 2024

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

2or2, resolution 1.84Å

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