1gue: Difference between revisions

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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
</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].
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Revision as of 01:49, 10 February 2016

SENSORY RHODOPSIN IISENSORY RHODOPSIN II

Structural highlights

1gue is a 1 chain structure with sequence from Atcc 35678. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

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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OCA