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1qat

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(New page: 200px<br /><applet load="1qat" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qat, resolution 3.0&Aring;" /> '''1-PHOSPHATIDYLINOSITO...)
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caption="1qat, resolution 3.0&Aring;" />
'''1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA COMPLEX WITH SAMARIUM (III) CHLORIDE'''<br />
'''1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA COMPLEX WITH SAMARIUM (III) CHLORIDE'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1QAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with SM as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QAT OCA].
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1QAT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=SM:'>SM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QAT OCA].
==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Grobler, J.A.]]
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[[Category: Grobler, J A.]]
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[[Category: Hurley, J.H.]]
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[[Category: Hurley, J H.]]
[[Category: SM]]
[[Category: SM]]
[[Category: calcium-binding]]
[[Category: calcium-binding]]
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[[Category: transducer]]
[[Category: transducer]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:32:29 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:41 2008''

Revision as of 12:37, 21 February 2008

Image:1qat.gif

1qat, resolution 3.0Å

Drag the structure with the mouse to rotate

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 with as ligand. Active as Phosphoinositide phospholipase C, with EC number 3.1.4.11 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 Feb 21 14:37:41 2008

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