1gue: Difference between revisions
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==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 [http://en.wikipedia.org/wiki/Atcc_35678 Atcc 35678]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GUE FirstGlance]. <br> | <table><tr><td colspan='2'>[[1gue]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35678 Atcc 35678]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GUE FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1gue" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1gue" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Bacteriorhodopsin 3D structures|Bacteriorhodopsin 3D structures]] | |||
*[[Rhodopsin|Rhodopsin]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 35678]] | [[Category: Atcc 35678]] | ||
[[Category: Large Structures]] | |||
[[Category: Edman, K]] | [[Category: Edman, K]] | ||
[[Category: Landau, E M]] | [[Category: Landau, E M]] | ||
Revision as of 12:08, 23 October 2019
SENSORY RHODOPSIN IISENSORY RHODOPSIN II
Structural highlights
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 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 |
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