3qdc

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<StructureSection load='3qdc' size='340' side='right'caption='[[3qdc]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='3qdc' size='340' side='right'caption='[[3qdc]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qdc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35678 Atcc 35678]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QDC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qdc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Natronomonas_pharaonis Natronomonas pharaonis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QDC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QDC 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=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=L2P:2,3-DI-PHYTANYL-GLYCEROL'>L2P</scene>, <scene name='pdbligand=LFA:EICOSANE'>LFA</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]] 2.5&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sop2, sopII ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2257 ATCC 35678])</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=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=L2P:2,3-DI-PHYTANYL-GLYCEROL'>L2P</scene>, <scene name='pdbligand=LFA:EICOSANE'>LFA</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=3qdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qdc OCA], [https://pdbe.org/3qdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qdc RCSB], [https://www.ebi.ac.uk/pdbsum/3qdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qdc 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=3qdc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qdc OCA], [https://pdbe.org/3qdc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qdc RCSB], [https://www.ebi.ac.uk/pdbsum/3qdc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qdc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/BACS2_NATPH BACS2_NATPH]] Involved in the control of phototaxis. Seems to activate a methyl-accepting protein (HTR-II). Photoreceptor for blue light.
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[https://www.uniprot.org/uniprot/BACS2_NATPH BACS2_NATPH] Involved in the control of phototaxis. Seems to activate a methyl-accepting protein (HTR-II). Photoreceptor for blue light.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The molecular mechanism of transmembrane signal transduction is still a pertinent question in cellular biology. Generally, a receptor can transfer an external signal via its cytoplasmic surface, as found for G-protein-coupled receptors such as rhodopsin, or via the membrane domain, such as that in sensory rhodopsin II (SRII) in complex with its transducer, HtrII. In the absence of HtrII, SRII functions as a proton pump. Here, we report on the crystal structure of the active state of uncomplexed SRII from Natronomonas pharaonis, NpSRII. The problem with a dramatic loss of diffraction quality upon loading of the active state was overcome by growing better crystals and by reducing the occupancy of the state. The conformational changes in the region comprising helices F and G are similar to those observed for the NpSRII-transducer complex but are much more pronounced. The meaning of these differences for the understanding of proton pumping and signal transduction by NpSRII is discussed.
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Active State of Sensory Rhodopsin II: Structural Determinants for Signal Transfer and Proton Pumping.,Gushchin I, Reshetnyak A, Borshchevskiy V, Ishchenko A, Round E, Grudinin S, Engelhard M, Buldt G, Gordeliy V J Mol Biol. 2011 Aug 4. PMID:21840321<ref>PMID:21840321</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 3qdc" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]]
*[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]]
*[[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: Atcc 35678]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Borshchevskiy, V]]
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[[Category: Natronomonas pharaonis]]
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[[Category: Buldt, G]]
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[[Category: Borshchevskiy V]]
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[[Category: Engelhard, M]]
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[[Category: Buldt G]]
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[[Category: Gordeliy, V]]
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[[Category: Engelhard M]]
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[[Category: Grudinin, S]]
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[[Category: Gordeliy V]]
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[[Category: Gushchin, I]]
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[[Category: Grudinin S]]
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[[Category: Ishchenko, A]]
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[[Category: Gushchin I]]
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[[Category: Reshetnyak, A]]
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[[Category: Ishchenko A]]
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[[Category: Round, E]]
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[[Category: Reshetnyak A]]
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[[Category: Membrane]]
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[[Category: Round E]]
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[[Category: Membrane protein]]
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[[Category: Nphtrii]]
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[[Category: Phototaxis]]
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Current revision

Crystal structure of Natronomonas pharaonis sensory rhodopsin II in the active state

PDB ID 3qdc

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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