1ah7: Difference between revisions

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[[Image:1ah7.gif|left|200px]]


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==PHOSPHOLIPASE C FROM BACILLUS CEREUS==
The line below this paragraph, containing "STRUCTURE_1ah7", creates the "Structure Box" on the page.
<StructureSection load='1ah7' size='340' side='right'caption='[[1ah7]], [[Resolution|resolution]] 1.50&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'>[[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>
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]] 1.501&#8491;</td></tr>
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<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>
{{STRUCTURE_1ah7| PDB=1ah7 |  SCENE= }}
<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>


'''PHOSPHOLIPASE C FROM BACILLUS CEREUS'''
==See Also==
 
*[[Lipase 3D Structures|Lipase 3D Structures]]
 
*[[Phospholipase C|Phospholipase C]]
==Overview==
__TOC__
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>
 
==About this Structure==
1AH7 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=1AH7 OCA].
 
==Reference==
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://www.ncbi.nlm.nih.gov/pubmed/2493587 2493587]
[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
[[Category: Phospholipase C]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Greaves R]]
[[Category: Greaves, R.]]
[[Category: Hydrolase]]
[[Category: Lipase]]
[[Category: Phospholipid hydrolysis]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:15:55 2008''

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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