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5ptd

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PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C MUTANT H32A

Structural highlights

5ptd is a 1 chain structure with sequence from Bacillus cereus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.7Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PLC_BACCE Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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., & 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.

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:9335537^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gassler CS, Ryan M, Liu T, Griffith OH, Heinz DW. Probing the roles of active site residues in phosphatidylinositol-specific phospholipase C from Bacillus cereus by site-directed mutagenesis. Biochemistry. 1997 Oct 21;36(42):12802-13. PMID:9335537 doi:10.1021/bi971102d

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ptd"

Categories: Bacillus cereus | Large Structures | Heinz DW

@@ Line 1: / Line 1: @@
 ==PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C MUTANT H32A==
-<StructureSection load='5ptd' size='340' side='right' caption='[[5ptd]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+<StructureSection load='5ptd' size='340' side='right'caption='[[5ptd]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ptd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5PTD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5PTD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ptd]] 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=5PTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5PTD FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PI-PLC GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 ATCC 14579])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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=5ptd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ptd OCA], [https://pdbe.org/5ptd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ptd RCSB], [https://www.ebi.ac.uk/pdbsum/5ptd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ptd ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ptd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ptd OCA], [http://pdbe.org/5ptd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ptd RCSB], [http://www.ebi.ac.uk/pdbsum/5ptd PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PLC_BACCE PLC_BACCE]] Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates.
+[https://www.uniprot.org/uniprot/PLC_BACCE PLC_BACCE] 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/pt/5ptd_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pt/5ptd_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 30: @@
 ==See Also==
+*[[Bromodomain-containing protein 3D structures|Bromodomain-containing protein 3D structures]]
 *[[Phospholipase C|Phospholipase C]]
 == References ==
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 14579]]
+[[Category: Bacillus cereus]]
-[[Category: Phosphatidylinositol diacylglycerol-lyase]]
+[[Category: Large Structures]]
-[[Category: Heinz, D W]]
+[[Category: Heinz DW]]
-[[Category: Hydrolase]]
-[[Category: Lipid degradation]]
-[[Category: Phosphatidylinositol specific phospholipase c]]
-[[Category: Phosphoric diester]]

5ptd

From Proteopedia

Current revision

PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C MUTANT H32A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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