3v00

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Current revision (14:12, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3v00' size='340' side='right'caption='[[3v00]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='3v00' size='340' side='right'caption='[[3v00]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3v00]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V00 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3v00]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V00 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V00 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GNAT1, GNAT1_BOVIN ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3v00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v00 OCA], [https://pdbe.org/3v00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v00 RCSB], [https://www.ebi.ac.uk/pdbsum/3v00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v00 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3v00 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v00 OCA], [https://pdbe.org/3v00 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v00 RCSB], [https://www.ebi.ac.uk/pdbsum/3v00 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v00 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/GNAT1_BOVIN GNAT1_BOVIN]] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase.
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[https://www.uniprot.org/uniprot/GNAT1_BOVIN GNAT1_BOVIN] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase.[https://www.uniprot.org/uniprot/GNAI1_RAT GNAI1_RAT] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.<ref>PMID:16870394</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The activation of Galpha subunits of heterotrimeric G proteins by G protein-coupled receptors (GPCRs) is a critical event underlying a variety of biological responses. Understanding how G proteins are activated will require structural and biochemical analyses of GPCRs complexed to their G protein partners, together with structure-function studies of Galpha mutants that shed light on the different steps in the activation pathway. Previously, we reported that the substitution of a glycine for a proline at position 56 within the linker region connecting the helical and GTP-binding domains of a Galpha chimera, designated alphaT*, yields a more readily exchangeable state for guanine nucleotides. Here we show that GDP-GTP exchange on alphaT*(G56P), in the presence of the light-activated GPCR, rhodopsin (R*), is less sensitive to the beta1gamma1 subunit complex than to wild-type alphaT*. We determined the X-ray crystal structure for the alphaT*(G56P) mutant and found that the G56P substitution leads to concerted changes that are transmitted to the conformationally sensitive switch regions, the alpha4-beta6 loop, and the beta6 strand. The alpha4-beta6 loop has been proposed to be a GPCR contact site that signals to the TCAT motif and weakens the binding of the guanine ring of GDP, whereas the switch regions are the contact sites for the beta1gamma1 complex. Collectively, these biochemical and structural data lead us to suggest that alphaT*(G56P) may be adopting a conformation that is normally induced within Galpha subunits by the combined actions of a GPCR and a Gbetagamma subunit complex during the G protein activation event.
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A constitutively active galpha subunit provides insights into the mechanism of g protein activation.,Singh G, Ramachandran S, Cerione RA Biochemistry. 2012 Apr 17;51(15):3232-40. Epub 2012 Apr 5. PMID:22448927<ref>PMID:22448927</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3v00" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bovin]]
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[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Cerione, R A]]
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[[Category: Rattus norvegicus]]
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[[Category: Singh, G]]
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[[Category: Cerione RA]]
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[[Category: Cell cycle]]
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[[Category: Singh G]]
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[[Category: Gtp binding]]
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[[Category: Gtpase]]
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[[Category: Signal transduction]]
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[[Category: Signaling protein]]
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[[Category: Transducer]]
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Current revision

Studies of a constitutively active G-alpha subunit provide insights into the mechanism of G protein activation.

PDB ID 3v00

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