1qas

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[[Image:1qas.gif|left|200px]]
[[Image:1qas.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1qas |SIZE=350|CAPTION= <scene name='initialview01'>1qas</scene>, resolution 2.4&Aring;
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The line below this paragraph, containing "STRUCTURE_1qas", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND=
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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/Phosphoinositide_phospholipase_C Phosphoinositide phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.11 3.1.4.11] </span>
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_1qas| PDB=1qas | 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=1qas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qas OCA], [http://www.ebi.ac.uk/pdbsum/1qas PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qas RCSB]</span>
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}}
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'''1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA 1'''
'''1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA 1'''
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[[Category: Grobler, J A.]]
[[Category: Grobler, J A.]]
[[Category: Hurley, J H.]]
[[Category: Hurley, J H.]]
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[[Category: calcium-binding]]
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[[Category: Calcium-binding]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: lipid degradation]]
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[[Category: Lipid degradation]]
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[[Category: transducer]]
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[[Category: Transducer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:04:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:11:07 2008''
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Revision as of 03:04, 3 May 2008

Image:1qas.gif

Template:STRUCTURE 1qas

1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA 1


Overview

The structure of the PH-domain truncated core of rat phosphoinositide-specific phospholipase C-delta 1 has been determined at 2.4 A resolution and compared to the structure previously determined in a different crystal form. The stereochemical relationship between the EF, catalytic, and C2 domains is essentially identical. The Ca2+ analogue Sm3+ binds at two sites between the jaws of the C2 domain. Sm3+ binding ejects three lysine residues which bridge the gap between the jaws and occupy the Ca2+ site in the apoenzyme, triggering a conformational change in the jaws. The distal sections of the C2 jaws move apart, opening the mouth by 9 A and creating a gap large enough to bind a phospholipid headgroup.

About this Structure

1QAS is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

C2 domain conformational changes in phospholipase C-delta 1., Grobler JA, Essen LO, Williams RL, Hurley JH, Nat Struct Biol. 1996 Sep;3(9):788-95. PMID:8784353 Page seeded by OCA on Sat May 3 06:04:38 2008

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