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3ptd

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[[Image:3ptd.jpg|left|200px]]<br /><applet load="3ptd" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="3ptd, resolution 2.2&Aring;" />
 
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'''PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C MUTANT D274S'''<br />
 
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==Overview==
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==PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C MUTANT D274S==
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The role of amino acid residues located in the active site pocket of, phosphatidylinositol-specific phospholipase C (PI-PLC) from Bacillus, cereus[Heinz, D. W., Ryan, M., Bullock, T., &amp; Griffith, O. H. (1995) EMBO, J. 14, 3855-3863] was investigated by site-directed mutagenesis, kinetics, and crystal structure analysis. Twelve residues involved in catalysis and, substrate binding (His32, Arg69, His82, Gly83, Lys115, Glu117, Arg163, Trp178, Asp180, Asp198, Tyr200, and Asp274) were individually replaced by, 1-3 other amino acids, resulting in a total number of 21 mutants., Replacements in the mutants H32A, H32L, R69A, R69E, R69K, H82A, H82L, E117K, R163I, D198A, D198E, D198S, Y200S, and D274S caused essentially, complete inactivation of the enzyme. The remaining mutants (G83S, K115E, R163K, W178Y, D180S, Y200F, and D274N) exhibited reduced activities up to, 57% when compared with wild-type PI-PLC. Crystal structures determined at, a resolution ranging from 2.0 to 2.7 A for six mutants (H32A, H32L, R163K, D198E, D274N, and D274S) showed that significant changes were confined to, the site of the respective mutation without perturbation of the rest of, the structure. Only in mutant D198E do the side chains of two neighboring, arginine residues move across the inositol binding pocket toward the newly, introduced glutamic acid. An analysis of these structure-function, relationships provides new insight into the catalytic mechanism, and, suggests a molecular explanation of some of the substrate, stereospecificity and inhibitor binding data available for this enzyme.
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<StructureSection load='3ptd' size='340' side='right'caption='[[3ptd]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3ptd]] 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=3PTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PTD 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ptd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ptd OCA], [https://pdbe.org/3ptd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ptd RCSB], [https://www.ebi.ac.uk/pdbsum/3ptd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ptd 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/pt/3ptd_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=3ptd 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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3PTD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_4.6.1.13 Transferred entry: 4.6.1.13], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.10 3.1.4.10] Known structural/functional Site: <scene name='pdbsite=ACT:Active+Site'>ACT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PTD 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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Probing the roles of active site residues in phosphatidylinositol-specific phospholipase C from Bacillus cereus by site-directed mutagenesis., Gassler CS, Ryan M, Liu T, Griffith OH, Heinz DW, Biochemistry. 1997 Oct 21;36(42):12802-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9335537 9335537]
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[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Transferred entry: 4.6.1.13]]
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[[Category: Heinz DW]]
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[[Category: Heinz, D.W.]]
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[[Category: hydrolase]]
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[[Category: lipid degradation]]
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[[Category: phosphatidylinositol specific phospholipase c]]
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[[Category: phosphoric diester]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:52:24 2008''
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Current revision

PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C MUTANT D274S

PDB ID 3ptd

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