1jad
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(New page: 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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Revision as of 21:14, 24 November 2007
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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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