2ptd: Difference between revisions

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[[Image:2ptd.gif|left|200px]]<br />
<applet load="2ptd" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2ptd, resolution 2.0&Aring;" />
'''PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C MUTANT D198E'''<br />


==Overview==
==PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C MUTANT D198E==
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='2ptd' size='340' side='right'caption='[[2ptd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ptd]] 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=2PTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PTD 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&#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=2ptd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ptd OCA], [https://pdbe.org/2ptd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ptd RCSB], [https://www.ebi.ac.uk/pdbsum/2ptd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ptd 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/2ptd_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=2ptd ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2PTD 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]]. Structure known Active Site: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2PTD 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: Transferred entry: 4.6.1.13]]
[[Category: Heinz DW]]
[[Category: Heinz, D.W.]]
[[Category: hydrolase]]
[[Category: lipid degradation]]
[[Category: phosphatidylinositol specific phospholipase c]]
[[Category: phosphoric diester]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 17:36:12 2007''

Latest revision as of 12:11, 21 February 2024

PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C MUTANT D198EPHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C MUTANT D198E

Structural highlights

2ptd 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 2Å
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.

See Also

2ptd, resolution 2.00Å

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