1gym

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(New page: 200px<br /><applet load="1gym" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gym, resolution 2.2&Aring;" /> '''PHOSPHATIDYLINOSITOL-...)
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[[Image:1gym.gif|left|200px]]<br /><applet load="1gym" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1gym, resolution 2.2&Aring;" />
 
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'''PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C IN COMPLEX WITH GLUCOSAMINE-(ALPHA-1-6)-MYO-INOSITOL'''<br />
 
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==Overview==
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==PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C IN COMPLEX WITH GLUCOSAMINE-(ALPHA-1-6)-MYO-INOSITOL==
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Numerous proteins on the external surface of the plasma membrane are, anchored by glycosylated derivatives of phosphatidylinositol (GPI), rather, than by hydrophobic amino acids embedded in the phospholipid bilayer., These GPI anchors are cleaved by phosphatidylinositol-specific, phospholipases C (PI-PLCs) to release a water-soluble protein with an, exposed glycosylinositol moiety and diacylglycerol, which remains in the, membrane. We have previously determined the crystal structure of Bacillus, cereus PI-PLC, the enzyme which is widely used to release GPI-anchored, proteins from membranes, as free enzyme and also in complex with, myo-inositol [Heinz, D.W., Ryan, M. Bullock, T.L., &amp; Griffith, O. H., (1995) EMBO J. 14, 3855-3863]. Here we report the refined 2.2 A crystal, structure of this enzyme complexed with a segment of the core of all GPI, anchors, glucosaminyl(alpha 1--&gt;6)-D-myo-inositol [GlcN-(alpha 1--&gt;6)Ins, ]. The myo-inositol moiety of GlcN(alpha 1--&gt;6)Ins is well-defined and, occupies essentially the same position in the active site as does free, myo-inositol, which provides convincing evidence that the enzyme utilizes, the same catalytic mechanism for cleavage of PI and GPI anchors. The, myo-inositol moiety makes several specific hydrogen bonding interactions, with active site residues. In contrast, the glucosamine moiety lies, exposed to solvent at the entrance of the active site with minimal, specific protein contacts. The glucosamine moiety is also less, well-defined, suggesting enhanced conformational flexibility. On the basis, of the positioning of GlcN(alpha 1--&gt;6)Ins in the active site, it is, predicted that the remainder of the GPI-glycan makes little or no specific, interactions with B. cereus PI-PLC. This explains why B. cereus PI-PLC can, cleave GPI anchors having variable glycan structures.
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<StructureSection load='1gym' size='340' side='right'caption='[[1gym]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1gym]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GYM 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]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYG:GLUCOSAMINYL-(ALPHA-6)-D-MYO-INOSITOL'>MYG</scene></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=1gym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gym OCA], [https://pdbe.org/1gym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gym RCSB], [https://www.ebi.ac.uk/pdbsum/1gym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gym ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PLC_BACCE PLC_BACCE] 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/gy/1gym_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=1gym 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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1GYM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus] with MYG as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1GYM 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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Crystal structure of phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with glucosaminyl(alpha 1--&gt;6)-D-myo-inositol, an essential fragment of GPI anchors., Heinz DW, Ryan M, Smith MP, Weaver LH, Keana JF, Griffith OH, Biochemistry. 1996 Jul 23;35(29):9496-504. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8755729 8755729]
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[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
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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: Griffith OH]]
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[[Category: Griffith, O.H.]]
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[[Category: Heinz DW]]
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[[Category: Heinz, D.W.]]
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[[Category: Keana JFW]]
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[[Category: Keana, J.F.W.]]
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[[Category: Ryan M]]
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[[Category: Ryan, M.]]
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[[Category: Smith MP]]
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[[Category: Smith, M.P.]]
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[[Category: Weaver LH]]
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[[Category: Weaver, L.H.]]
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[[Category: MYG]]
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[[Category: glucosaminyl (alpha-1-6)-d-myo-inositol]]
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[[Category: hydrolase (phosphoric diester)]]
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[[Category: inhibitor complex]]
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[[Category: lipid degradation]]
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[[Category: phosphatidylinositol specific phospholipase c]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:21:03 2007''
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Current revision

PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C IN COMPLEX WITH GLUCOSAMINE-(ALPHA-1-6)-MYO-INOSITOL

PDB ID 1gym

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