3am6

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<StructureSection load='3am6' size='340' side='right'caption='[[3am6]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='3am6' size='340' side='right'caption='[[3am6]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3am6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aceat Aceat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AM6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3am6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetabularia_acetabulum Acetabularia acetabulum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AM6 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=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=RET:RETINAL'>RET</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]] 3.2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1c3w|1c3w]], [[1xio|1xio]]</div></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=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=RET:RETINAL'>RET</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=3am6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3am6 OCA], [https://pdbe.org/3am6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3am6 RCSB], [https://www.ebi.ac.uk/pdbsum/3am6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3am6 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=3am6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3am6 OCA], [https://pdbe.org/3am6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3am6 RCSB], [https://www.ebi.ac.uk/pdbsum/3am6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3am6 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/G1K3Q0_ACEAT G1K3Q0_ACEAT]
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Acetabularia rhodopsin (AR) is a rhodopsin from the marine plant Acetabularia acetabulum. The opsin-encoding gene from A. acetabulum, ARII, was cloned and found to be novel but homologous to that reported previously. ARII is a light-driven proton pump, as demonstrated by the existence of a photo-induced current through Xenopus oocytes expressing ARII. The photochemical reaction of ARII prepared by cell-free protein synthesis was similar to that of bacteriorhodopsin (BR), except for the lack of light-dark adaptation and the different proton release and uptake sequence. The crystal structure determined at 3.2 A resolution is the first structure of a eukaryotic member of the microbial rhodopsin family. The structure of ARII is similar to that of BR. From the cytoplasmic side to the extracellular side of the proton transfer pathway in ARII, Asp92, a Schiff base, Asp207, Asp81, Arg78, Glu199, and Ser189 are arranged in positions similar to those of the corresponding residues directly involved in proton transfer by BR. The side-chain carboxyl group of Asp92 appears to interact with the sulfhydryl group of Cys218, which is unique to ARII and corresponds to Leu223 of BR and to Asp217 of Anabaena sensory rhodopsin. The orientation of the Arg78 side chain is opposite to the corresponding Arg82 of BR. The putative absence of water molecules around Glu199 and Arg78 may disrupt the formation of the low-barrier hydrogen bond at Glu199, resulting in the "late proton release".
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Crystal structure of the eukaryotic light-driven proton-pumping rhodopsin, Acetabularia rhodopsin II, from marine alga.,Wada T, Shimono K, Kikukawa T, Hato M, Shinya N, Kim SY, Kimura-Someya T, Shirouzu M, Tamogami J, Miyauchi S, Jung KH, Kamo N, Yokoyama S J Mol Biol. 2011 Sep 2;411(5):986-98. Epub 2011 Jun 25. PMID:21726566<ref>PMID:21726566</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 3am6" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Rhodopsin 3D structures|Rhodopsin 3D structures]]
*[[Rhodopsin 3D structures|Rhodopsin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aceat]]
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[[Category: Acetabularia acetabulum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Wada, T]]
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[[Category: Wada T]]
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[[Category: Yokoyama, S]]
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[[Category: Yokoyama S]]
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[[Category: Seven trans-membrane]]
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[[Category: Transport protein]]
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Revision as of 08:40, 7 February 2024

Crystal structure of the proton pumping rhodopsin AR2 from marine alga Acetabularia acetabulum

PDB ID 3am6

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