2iia

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Current revision (09:03, 21 February 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2iia]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IIA FirstGlance]. <br>
<table><tr><td colspan='2'>[[2iia]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IIA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IIA FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ii7|2ii7]], [[2ii8|2ii8]], [[2ii9|2ii9]]</div></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]] 1.8&#8491;</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=2iia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iia OCA], [https://pdbe.org/2iia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iia RCSB], [https://www.ebi.ac.uk/pdbsum/2iia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iia 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=2iia FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iia OCA], [https://pdbe.org/2iia PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iia RCSB], [https://www.ebi.ac.uk/pdbsum/2iia PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iia ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8YSC3_NOSS1 Q8YSC3_NOSS1]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2iia 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=2iia ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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We present crystal structures of the Anabaena sensory rhodopsin transducer (ASRT), a soluble cytoplasmic protein that interacts with the first structurally characterized eubacterial retinylidene photoreceptor Anabaena sensory rhodopsin (ASR). Four crystal structures of ASRT from three different spacegroups were obtained, in all of which ASRT is present as a planar (C4) tetramer, consistent with our characterization of ASRT as a tetramer in solution. The ASRT tetramer is tightly packed, with large interfaces where the well-structured beta-sandwich portion of the monomers provides the bulk of the tetramer-forming interactions, and forms a flat, stable surface on one side of the tetramer (the beta-face). Only one of our four different ASRT crystals reveals a C-terminal alpha-helix in the otherwise all-beta protein, together with a large loop from each monomer on the opposite face of the tetramer (the alpha-face), which is flexible and largely disordered in the other three crystal forms. Gel-filtration chromatography demonstrated that ASRT forms stable tetramers in solution and isothermal microcalorimetry showed that the ASRT tetramer binds to ASR with a stoichiometry of one ASRT tetramer per one ASR photoreceptor with a K(d) of 8 microM in the highest affinity measurements. Possible mechanisms for the interaction of this transducer tetramer with the ASR photoreceptor via its flexible alpha-face to mediate transduction of the light signal are discussed.
 
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Crystal structure of the Anabaena sensory rhodopsin transducer.,Vogeley L, Trivedi VD, Sineshchekov OA, Spudich EN, Spudich JL, Luecke H J Mol Biol. 2007 Mar 30;367(3):741-51. Epub 2006 Dec 1. PMID:17289074<ref>PMID:17289074</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 2iia" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Anabaena sp]]
[[Category: Anabaena sp]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Luecke, H]]
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[[Category: Luecke H]]
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[[Category: Sineshchekov, O A]]
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[[Category: Sineshchekov OA]]
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[[Category: Spudich, E N]]
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[[Category: Spudich EN]]
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[[Category: Spudich, J L]]
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[[Category: Spudich JL]]
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[[Category: Trivedi, V D]]
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[[Category: Trivedi VD]]
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[[Category: Vogeley, L]]
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[[Category: Vogeley L]]
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[[Category: Rhodopsin]]
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[[Category: Signaling protein]]
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[[Category: Transducer]]
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Current revision

Anabaena sensory rhodopsin transducer

PDB ID 2iia

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