1ptd: Difference between revisions

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[[Image:1ptd.jpg|left|200px]]


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==PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C==
The line below this paragraph, containing "STRUCTURE_1ptd", creates the "Structure Box" on the page.
<StructureSection load='1ptd' size='340' side='right'caption='[[1ptd]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1ptd]] 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=1PTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PTD FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#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=1ptd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ptd OCA], [https://pdbe.org/1ptd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ptd RCSB], [https://www.ebi.ac.uk/pdbsum/1ptd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ptd ProSAT]</span></td></tr>
{{STRUCTURE_1ptd| PDB=1ptd |  SCENE= }}
</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/1ptd_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=1ptd ConSurf].
<div style="clear:both"></div>


'''PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C'''
==See Also==
 
*[[Phospholipase C|Phospholipase C]]
 
__TOC__
==Overview==
</StructureSection>
Phosphatidylinositol (PI), once regarded as an obscure component of membranes, is now recognized as an important reservoir of second messenger precursors and as an anchor for membrane enzymes. PI-specific phospholipase C (PI-PLC) is the enzyme that cleaves PI, invoking numerous cellular responses. The crystal structure of PI-PLC from Bacillus cereus (EC 3.1.4.10) has been solved at 2.6 A resolution and refined to a crystallographic R factor of 18.7%. The structure consists of an imperfect (beta alpha)8-barrel similar to that first observed for triose phosphate isomerase and does not resemble any other known phospholipase structure. The active site of the enzyme has been identified by determining the structure of PI-PLC in complex with its inhibitor, myo-inositol, at 2.6 A resolution (R factor = 19.5%). This substrate-like inhibitor interacts with a number of residues highly conserved among prokaryotic PI-PLCs. Residues His32 and His82, which are also conserved between prokaryotic and eukaryotic PI-PLCs, most likely act as general base and acid respectively in a catalytic mechanism analogous to that observed for ribonucleases.
 
==About this Structure==
1PTD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PTD OCA].
 
==Reference==
Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol., Heinz DW, Ryan M, Bullock TL, Griffith OH, EMBO J. 1995 Aug 15;14(16):3855-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7664726 7664726]
[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
[[Category: Phosphatidylinositol diacylglycerol-lyase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Bullock TL]]
[[Category: Bullock, T L.]]
[[Category: Griffith OH]]
[[Category: Griffith, O H.]]
[[Category: Heinz DW]]
[[Category: Heinz, D W.]]
[[Category: Ryan M]]
[[Category: Ryan, M.]]
[[Category: Hydrolase]]
[[Category: Phosphatidylinositol specific phospholipase c]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 05:27:59 2008''

Latest revision as of 11:10, 14 February 2024

PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE CPHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C

Structural highlights

1ptd 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 2.6Å
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

1ptd, resolution 2.60Å

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