4ptd: Difference between revisions

New page: left|200px<br /> <applet load="4ptd" size="450" color="white" frame="true" align="right" spinBox="true" caption="4ptd, resolution 2.3Å" /> '''PHOSPHATIDYLINOSITOL...
 
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[[Image:4ptd.gif|left|200px]]<br />
<applet load="4ptd" size="450" color="white" frame="true" align="right" spinBox="true"
caption="4ptd, resolution 2.3&Aring;" />
'''PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C MUTANT D274N'''<br />


==Overview==
==PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C MUTANT D274N==
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, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9335537 (full description)]]
<StructureSection load='4ptd' size='340' side='right'caption='[[4ptd]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ptd]] 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=4PTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PTD 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]] 2.3&#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=4ptd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ptd OCA], [https://pdbe.org/4ptd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ptd RCSB], [https://www.ebi.ac.uk/pdbsum/4ptd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ptd ProSAT]</span></td></tr>
</table>
== Function ==
[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/4ptd_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=4ptd ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
4PTD 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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.10 3.1.4.10]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=4PTD OCA]].
*[[Phospholipase C|Phospholipase C]]
 
__TOC__
==Reference==
</StructureSection>
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]
[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Heinz, D.W.]]
[[Category: Heinz DW]]
[[Category: hydrolase]]
[[Category: lipid degradation]]
[[Category: phosphatidylinositol specific phospholipase c]]
[[Category: phosphoric diester]]
 
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