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[[Image:1gue.gif|left|200px]]


{{Structure
==SENSORY RHODOPSIN II==
|PDB= 1gue |SIZE=350|CAPTION= <scene name='initialview01'>1gue</scene>, resolution 2.27&Aring;
<StructureSection load='1gue' size='340' side='right'caption='[[1gue]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
|SITE= <scene name='pdbsite=RET:Cl+Binding+Site+For+Chain+A'>RET</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene>
<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>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.27&#8491;</td></tr>
|GENE=  
<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>
|DOMAIN=
<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>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gue OCA], [http://www.ebi.ac.uk/pdbsum/1gue PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gue RCSB]</span>
== 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 ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <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/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=1gue ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sensory 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.


'''SENSORY RHODOPSIN II'''
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<ref>PMID:11937052</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1gue" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Sensory 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.
*[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]]
 
*[[Rhodopsin 3D structures|Rhodopsin 3D structures]]
==About this Structure==
== References ==
1GUE is a [[Single protein]] structure of sequence from [http://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].
<references/>
 
__TOC__
==Reference==
</StructureSection>
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:[http://www.ncbi.nlm.nih.gov/pubmed/11937052 11937052]
[[Category: Large Structures]]
[[Category: Natronomonas pharaonis]]
[[Category: Natronomonas pharaonis]]
[[Category: Single protein]]
[[Category: Edman K]]
[[Category: Edman, K.]]
[[Category: Landau EM]]
[[Category: Landau, E M.]]
[[Category: Maxwell CA]]
[[Category: Maxwell, C A.]]
[[Category: Navarro J]]
[[Category: Navarro, J.]]
[[Category: Neutze R]]
[[Category: Neutze, R.]]
[[Category: Nollert P]]
[[Category: Nollert, P.]]
[[Category: Pebay-Peyroula E]]
[[Category: Pebay-Peyroula, E.]]
[[Category: Royant A]]
[[Category: Royant, A.]]
[[Category: archaeal rhodopsin]]
[[Category: photoreceptor]]
[[Category: phototaxis]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:51:26 2008''

Latest revision as of 03:01, 21 November 2024

SENSORY RHODOPSIN IISENSORY RHODOPSIN II

Structural highlights

1gue is a 1 chain structure with sequence from Natronomonas pharaonis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.27Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BACS2_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 PubMed

Sensory 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 Also

References

  1. ↑ Edman K, Royant A, Nollert P, Maxwell CA, Pebay-Peyroula E, Navarro J, Neutze R, Landau EM. Early structural rearrangements in the photocycle of an integral membrane sensory receptor. Structure. 2002 Apr;10(4):473-82. PMID:11937052

1gue, resolution 2.27Å

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