1ah7

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[[Image:1ah7.gif|left|200px]]
[[Image:1ah7.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1ah7 |SIZE=350|CAPTION= <scene name='initialview01'>1ah7</scene>, resolution 1.501&Aring;
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The line below this paragraph, containing "STRUCTURE_1ah7", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=CAT:Catalytic+Site,+Substrate+Binding'>CAT</scene>, <scene name='pdbsite=ZNA:Zn+Coordination+Site'>ZNA</scene>, <scene name='pdbsite=ZNB:Zn+Coordination+Site'>ZNB</scene> and <scene name='pdbsite=ZNC:Zn+Coordination+Site'>ZNC</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1ah7| PDB=1ah7 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ah7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ah7 OCA], [http://www.ebi.ac.uk/pdbsum/1ah7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ah7 RCSB]</span>
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}}
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'''PHOSPHOLIPASE C FROM BACILLUS CEREUS'''
'''PHOSPHOLIPASE C FROM BACILLUS CEREUS'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Greaves, R.]]
[[Category: Greaves, R.]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: lipase]]
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[[Category: Lipase]]
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[[Category: phospholipid hydrolysis]]
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[[Category: Phospholipid hydrolysis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:15:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:40:07 2008''
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Revision as of 07:15, 2 May 2008

Image:1ah7.gif

Template:STRUCTURE 1ah7

PHOSPHOLIPASE C FROM BACILLUS CEREUS


Overview

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.

About this Structure

1AH7 is a Single protein structure of sequence from Bacillus cereus. Full crystallographic information is available from 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:2493587 Page seeded by OCA on Fri May 2 10:15:55 2008

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