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[[Image:1ah7.gif|left|200px]]<br />
<applet load="1ah7" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ah7, resolution 1.501&Aring;" />
'''PHOSPHOLIPASE C FROM BACILLUS CEREUS'''<br />


==Overview==
==PHOSPHOLIPASE C FROM BACILLUS CEREUS==
Both the phosphatidylinositol-hydrolysing and the, phosphatidylcholine-hydrolysing phospholipases C have been implicated in, the generation of second messengers in mammalian cells. The, phosphatidylcholine-hydrolysing phospholipase C (PLC) from Bacillus, cereus, a monomeric protein containing 245 amino-acid residues, is similar, to some of the corresponding mammalian proteins. This, together with the, fact that the bacterial enzyme can mimic the action of mammalian PLC in, causing, for example, enhanced prostaglandin biosynthesis, suggests that, B. cereus PLC can be used as a model for the hitherto poorly characterized, mammalian PLCs. We report here the three-dimensional structure of B., cereus PLC at 1.5 A resolution. The enzyme is an all-helix protein, belonging to a novel structural class and contains, at least in the, crystalline state, three Zn2+ in the active site. We also present, preliminary results from a study at 1.9 A resolution of the complex, between PLC and inorganic phosphate (Pi) which indicate that the substrate, binds directly to the metal ions.
<StructureSection load='1ah7' size='340' side='right'caption='[[1ah7]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ah7]] 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=1AH7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AH7 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]] 1.501&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1ah7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ah7 OCA], [https://pdbe.org/1ah7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ah7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ah7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ah7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PHLC_BACCE PHLC_BACCE] Required, with sphingomyelinase, to effect target cell lysis (hemolysis).
== 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/ah/1ah7_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=1ah7 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1AH7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Phospholipase_C Phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.3 3.1.4.3] Structure known Active Sites: CAT, ZNA, ZNB and ZNC. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AH7 OCA].
*[[Lipase 3D Structures|Lipase 3D Structures]]
 
*[[Phospholipase C|Phospholipase C]]
==Reference==
__TOC__
High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus., Hough E, Hansen LK, Birknes B, Jynge K, Hansen S, Hordvik A, Little C, Dodson E, Derewenda Z, Nature. 1989 Mar 23;338(6213):357-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2493587 2493587]
</StructureSection>
[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
[[Category: Phospholipase C]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Greaves R]]
[[Category: Greaves, R.]]
[[Category: ZN]]
[[Category: hydrolase]]
[[Category: lipase]]
[[Category: phospholipid hydrolysis]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 15:47:52 2007''

Latest revision as of 09:30, 7 February 2024

PHOSPHOLIPASE C FROM BACILLUS CEREUSPHOSPHOLIPASE C FROM BACILLUS CEREUS

Structural highlights

1ah7 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 1.501Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PHLC_BACCE Required, with sphingomyelinase, to effect target cell lysis (hemolysis).

Evolutionary Conservation

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

See Also

1ah7, resolution 1.50Å

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