1gue: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (7 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==SENSORY RHODOPSIN II== | ==SENSORY RHODOPSIN II== | ||
<StructureSection load='1gue' size='340' side='right' caption='[[1gue]], [[Resolution|resolution]] 2.27Å' scene=''> | <StructureSection load='1gue' size='340' side='right'caption='[[1gue]], [[Resolution|resolution]] 2.27Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gue]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1gue]] 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=1GUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GUE FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.27Å</td></tr> | ||
<tr><td class="sblockLbl"><b>[[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gue OCA], [https://pdbe.org/1gue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gue RCSB], [https://www.ebi.ac.uk/pdbsum/1gue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gue ProSAT]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[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. | |||
== 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/gu/1gue_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gu/1gue_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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/ | </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=1gue ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 25: | Line 28: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1gue" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Bacteriorhodopsin|Bacteriorhodopsin]] | *[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]] | ||
*[[Rhodopsin|Rhodopsin]] | *[[Rhodopsin 3D structures|Rhodopsin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Natronomonas pharaonis]] | [[Category: Natronomonas pharaonis]] | ||
[[Category: Edman | [[Category: Edman K]] | ||
[[Category: Landau | [[Category: Landau EM]] | ||
[[Category: Maxwell | [[Category: Maxwell CA]] | ||
[[Category: Navarro | [[Category: Navarro J]] | ||
[[Category: Neutze | [[Category: Neutze R]] | ||
[[Category: Nollert | [[Category: Nollert P]] | ||
[[Category: Pebay-Peyroula | [[Category: Pebay-Peyroula E]] | ||
[[Category: Royant | [[Category: Royant A]] | ||
Latest revision as of 03:01, 21 November 2024
SENSORY RHODOPSIN IISENSORY RHODOPSIN II
Structural highlights
FunctionBACS2_NATPH Involved in the control of phototaxis. Seems to activate a methyl-accepting protein (HTR-II). Photoreceptor for blue light. 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 PubMedSensory rhodopsins are the primary receptors of vision in animals and phototaxis in microorganisms. Light triggers the rapid isomerization of a buried retinal chromophore, which the protein both accommodates and amplifies into the larger structural rearrangements required for signaling. We trapped an early intermediate of the photocycle of sensory rhodopsin II from Natronobacterium pharaonis (pSRII) in 3D crystals and determined its X-ray structure to 2.3 A resolution. The observed structural rearrangements were localized near the retinal chromophore, with a key water molecule becoming disordered and the retinal's beta-ionone ring undergoing a prominent movement. Comparison with the early structural rearrangements of bacteriorhodopsin illustrates how modifications in the retinal binding pocket of pSRII allow subtle differences in the early relaxation of photoisomerized retinal. Early structural rearrangements in the photocycle of an integral membrane sensory receptor.,Edman K, Royant A, Nollert P, Maxwell CA, Pebay-Peyroula E, Navarro J, Neutze R, Landau EM Structure. 2002 Apr;10(4):473-82. PMID:11937052[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||||