1suj: Difference between revisions

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==X-ray crystal structure of ambystoma tigrinum cone arrestin==
==X-ray crystal structure of ambystoma tigrinum cone arrestin==
<StructureSection load='1suj' size='340' side='right' caption='[[1suj]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
<StructureSection load='1suj' size='340' side='right'caption='[[1suj]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1suj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ambystoma_tigrinum Ambystoma tigrinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SUJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1suj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ambystoma_tigrinum Ambystoma tigrinum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SUJ FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cf1|1cf1]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.38&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8305 Ambystoma tigrinum])</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=1suj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1suj OCA], [https://pdbe.org/1suj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1suj RCSB], [https://www.ebi.ac.uk/pdbsum/1suj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1suj ProSAT]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1suj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1suj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1suj RCSB], [http://www.ebi.ac.uk/pdbsum/1suj PDBsum]</span></td></tr>
</table>
<table>
== Function ==
[https://www.uniprot.org/uniprot/Q9PTE7_AMBTI Q9PTE7_AMBTI]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/su/1suj_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/su/1suj_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=1suj ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 1suj" style="background-color:#fffaf0;"></div>
==See Also==
*[[Arrestin 3D structures|Arrestin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Ambystoma tigrinum]]
[[Category: Ambystoma tigrinum]]
[[Category: Navarro, J.]]
[[Category: Large Structures]]
[[Category: Sutton, R B.]]
[[Category: Navarro J]]
[[Category: Sensory transduction]]
[[Category: Sutton RB]]
[[Category: Signaling protein]]

Latest revision as of 09:20, 23 August 2023

X-ray crystal structure of ambystoma tigrinum cone arrestinX-ray crystal structure of ambystoma tigrinum cone arrestin

Structural highlights

1suj is a 1 chain structure with sequence from Ambystoma tigrinum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.38Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9PTE7_AMBTI

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Arrestins play a fundamental role in the regulation and signal transduction of G protein-coupled receptors. Here we describe the crystal structure of cone arrestin at 2.3A resolution. The overall structure of cone visual arrestin is similar to the crystal structures of rod visual and the non-visual arrestin-2, consisting of two domains, each containing ten beta-sheets. However, at the tertiary structure level, there are two major differences, in particular on the concave surfaces of the two domains implicated in receptor binding and in the loop between beta-strands I and II. Functional analysis shows that cone arrestin, in sharp contrast to its rod counterpart, bound cone pigments and non-visual receptors. Conversely, non-visual arrestin-2 bound cone pigments, suggesting that it may also regulate phototransduction and/or photopigment trafficking in cone photoreceptors. These findings indicate that cone arrestin displays structural and functional features intermediate between the specialized rod arrestin and the non-visual arrestins, which have broad receptor specificity. A unique functional feature of cone arrestin was the low affinity for its cognate receptor, resulting in an unusually rapid dissociation of the complex. Transient arrestin binding to the photopigment in cones may be responsible for the extremely rapid regeneration and reuse of the photopigment that is essential for cone function at high levels of illumination.

Crystal structure of cone arrestin at 2.3A: evolution of receptor specificity.,Sutton RB, Vishnivetskiy SA, Robert J, Hanson SM, Raman D, Knox BE, Kono M, Navarro J, Gurevich VV J Mol Biol. 2005 Dec 16;354(5):1069-80. Epub 2005 Nov 2. PMID:16289201[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Sutton RB, Vishnivetskiy SA, Robert J, Hanson SM, Raman D, Knox BE, Kono M, Navarro J, Gurevich VV. Crystal structure of cone arrestin at 2.3A: evolution of receptor specificity. J Mol Biol. 2005 Dec 16;354(5):1069-80. Epub 2005 Nov 2. PMID:16289201 doi:10.1016/j.jmb.2005.10.023

1suj, resolution 2.38Å

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OCA