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1qat
From Proteopedia
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| , resolution 3.0Å | |||||||
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| Ligands: | |||||||
| Activity: | Phosphoinositide phospholipase C, with EC number 3.1.4.11 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA COMPLEX WITH SAMARIUM (III) CHLORIDE
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
1QAT 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 Thu Mar 20 13:35:11 2008
