1jad: Difference between revisions
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[[Image:1jad.gif|left|200px]] | [[Image:1jad.gif|left|200px]] | ||
'''C-terminal Domain of Turkey PLC-beta''' | {{Structure | ||
|PDB= 1jad |SIZE=350|CAPTION= <scene name='initialview01'>1jad</scene>, resolution 2.40Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''C-terminal Domain of Turkey PLC-beta''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1JAD is a [ | 1JAD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JAD OCA]. | ||
==Reference== | ==Reference== | ||
A unique fold of phospholipase C-beta mediates dimerization and interaction with G alpha q., Singer AU, Waldo GL, Harden TK, Sondek J, Nat Struct Biol. 2002 Jan;9(1):32-6. PMID:[http:// | A unique fold of phospholipase C-beta mediates dimerization and interaction with G alpha q., Singer AU, Waldo GL, Harden TK, Sondek J, Nat Struct Biol. 2002 Jan;9(1):32-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11753430 11753430] | ||
[[Category: Meleagris gallopavo]] | [[Category: Meleagris gallopavo]] | ||
[[Category: Phosphoinositide phospholipase C]] | [[Category: Phosphoinositide phospholipase C]] | ||
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[[Category: alpha helical coiled coil]] | [[Category: alpha helical coiled coil]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:00:42 2008'' | ||
Revision as of 10:00, 20 March 2008
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| 1jad, resolution 2.40Å | |||||||||||||
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| Ligands: | SO4 | ||||||||||||
| Activity: | Phosphoinositide phospholipase C, with EC number 3.1.4.11 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
C-terminal Domain of Turkey PLC-beta
Overview
GTP-bound subunits of the Gq family of G alpha subunits directly activate phospholipase C-beta (PLC-beta) isozymes to produce the second messengers inositol 1,4,5-trisphosphate and diacylglycerol. PLC-betas are GTPase activating proteins (GAPs) that also promote the formation of GDP-bound, inactive G beta subunits. Both phospholipase activation by G alpha-GTP subunits and GAP activity require a C-terminal region unique to PLC-beta isozymes. The crystal structure of the C-terminal region from an avian PLC-beta, determined at 2.4 A resolution, reveals a novel fold composed almost entirely of three long helices forming a coiled-coil that dimerizes along its long axis in an antiparallel orientation. The dimer interface is extensive ( approximately 3,200 A(2)), and, based on gel exclusion chromatography, full length PLC-betas are dimeric, indicating that PLC-betas likely function as dimers. Sequence conservation, mutational data and molecular modeling show that an electrostatically positive surface of the dimer contains the major determinants for binding G beta q. Effector dimerization, as highlighted by PLC-betas, provides a viable mechanism for regulating signaling cascades linked to heterotrimeric G proteins.
About this Structure
1JAD is a Single protein structure of sequence from Meleagris gallopavo. Full crystallographic information is available from OCA.
Reference
A unique fold of phospholipase C-beta mediates dimerization and interaction with G alpha q., Singer AU, Waldo GL, Harden TK, Sondek J, Nat Struct Biol. 2002 Jan;9(1):32-6. PMID:11753430
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