1qas: Difference between revisions
New page: left|200px<br /><applet load="1qas" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qas, resolution 2.4Å" /> '''1-PHOSPHATIDYLINOSITO... |
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[[Image:1qas.gif|left|200px]]<br /><applet load="1qas" size=" | [[Image:1qas.gif|left|200px]]<br /><applet load="1qas" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1qas, resolution 2.4Å" /> | caption="1qas, resolution 2.4Å" /> | ||
'''1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA 1'''<br /> | '''1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA 1'''<br /> | ||
==Overview== | ==Overview== | ||
The structure of the PH-domain truncated core of rat | 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== | ||
1QAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. 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:// | 1QAS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. 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=1QAS OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Grobler, J | [[Category: Grobler, J A.]] | ||
[[Category: Hurley, J | [[Category: Hurley, J H.]] | ||
[[Category: calcium-binding]] | [[Category: calcium-binding]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: transducer]] | [[Category: transducer]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:39 2008'' | ||
Revision as of 15:37, 21 February 2008
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1-PHOSPHATIDYLINOSITOL-4,5-BISPHOSPHATE PHOSPHODIESTERASE DELTA 1
OverviewOverview
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 StructureAbout this Structure
1QAS is a Single protein structure of sequence from Rattus norvegicus. Active as Phosphoinositide phospholipase C, with EC number 3.1.4.11 Full crystallographic information is available from OCA.
ReferenceReference
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
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