This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1fqi

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

RGS9 RGS DOMAIN

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fqi"

@@ Line 1: / Line 1: @@
-[[Image:1fqi.gif|left|200px]]<br /><applet load="1fqi" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1fqi, resolution 1.94&Aring;" />
-'''RGS9 RGS DOMAIN'''<br />
-==Overview==
+==RGS9 RGS DOMAIN==
-A multitude of heptahelical receptors use heterotrimeric G proteins to, transduce signals to specific effector target molecules. The G protein, transducin, Gt, couples photon-activated rhodopsin with the effector, cyclic GMP phosophodiesterase (PDE) in the vertebrate phototransduction, cascade. The interactions of the Gt alpha-subunit (alpha(t)) with the, inhibitory PDE gamma-subunit (PDEgamma) are central to effector, activation, and also enhance visual recovery in cooperation with the, GTPase-activating protein regulator of G-protein signalling (RGS)-9 (refs, 1-3). Here we describe the crystal structure at 2.0 A of rod transducin, alpha x GDP x AlF4- in complex with the effector molecule PDEgamma and the, GTPase-activating protein RGS9. In addition, we present the independently, solved crystal structures of the RGS9 RGS domain both alone and in complex, with alpha(t/i1) x GDP x AlF4-. These structures reveal insights into, effector activation, synergistic GTPase acceleration, RGS9 specificity and, RGS activity. Effector binding to a nucleotide-dependent site on alpha(t), sequesters PDEgamma residues implicated in PDE inhibition, and potentiates, recruitment of RGS9 for hydrolytic transition state stabilization and, concomitant signal termination.
+<StructureSection load='1fqi' size='340' side='right'caption='[[1fqi]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1fqi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FQI FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1fqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fqi OCA], [https://pdbe.org/1fqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fqi RCSB], [https://www.ebi.ac.uk/pdbsum/1fqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fqi ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/RGS9_BOVIN RGS9_BOVIN] Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to G(t)-alpha. Involved in phototransduction; key element in the recovery phase of visual transduction.
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fq/1fqi_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fqi ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-FQI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FQI OCA].
+*[[Regulator of G-protein signaling 3D structures|Regulator of G-protein signaling 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A., Slep KC, Kercher MA, He W, Cowan CW, Wensel TG, Sigler PB, Nature. 2001 Feb 22;409(6823):1071-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11234020 11234020]
 [[Category: Bos taurus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Cowan, C.W.]]
+[[Category: Cowan CW]]
-[[Category: He, W.]]
+[[Category: He W]]
-[[Category: Kercher, M.A.]]
+[[Category: Kercher MA]]
-[[Category: Sigler, P.B.]]
+[[Category: Sigler PB]]
-[[Category: Slep, K.C.]]
+[[Category: Slep KC]]
-[[Category: Wensel, T.G.]]
+[[Category: Wensel TG]]
-[[Category: gap]]
-[[Category: phototransduction]]
-[[Category: rgs]]
-[[Category: rgs9]]
-[[Category: rod]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:09:52 2007''

1fqi

From Proteopedia

Current revision

RGS9 RGS DOMAIN

Structural highlights

Function

Evolutionary Conservation

See Also

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox