1jad: Difference between revisions
New page: left|200px<br /><applet load="1jad" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jad, resolution 2.40Å" /> '''C-terminal Domain of... |
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[[Image:1jad.gif|left|200px]]<br /><applet load="1jad" size=" | [[Image:1jad.gif|left|200px]]<br /><applet load="1jad" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1jad, resolution 2.40Å" /> | caption="1jad, resolution 2.40Å" /> | ||
'''C-terminal Domain of Turkey PLC-beta'''<br /> | '''C-terminal Domain of Turkey PLC-beta'''<br /> | ||
==Overview== | ==Overview== | ||
GTP-bound subunits of the Gq family of G alpha subunits directly activate | 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== | ==About this Structure== | ||
1JAD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo] with SO4 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:// | 1JAD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Meleagris_gallopavo Meleagris gallopavo] with <scene name='pdbligand=SO4:'>SO4</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=1JAD OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Phosphoinositide phospholipase C]] | [[Category: Phosphoinositide phospholipase C]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Harden, T | [[Category: Harden, T K.]] | ||
[[Category: Singer, A | [[Category: Singer, A U.]] | ||
[[Category: Sondek, J.]] | [[Category: Sondek, J.]] | ||
[[Category: Waldo, G | [[Category: Waldo, G L.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: alpha helical coiled coil]] | [[Category: alpha helical coiled coil]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:20:27 2008'' | ||
Revision as of 11:20, 21 February 2008
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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 with SO4 as ligand. Active as Phosphoinositide phospholipase C, with EC number 3.1.4.11 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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