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1JGJ

CRYSTAL STRUCTURE OF SENSORY RHODOPSIN II AT 2.4 ANGSTROMS: INSIGHTS INTO COLOR TUNING AND TRANSDUCER INTERACTION

Summary for 1JGJ
Entry DOI10.2210/pdb1jgj/pdb
Related1c3w
DescriptorSENSORY RHODOPSIN II, octyl beta-D-glucopyranoside, RETINAL, ... (4 entities in total)
Functional Keywordssensory rhodopsin, membrane protein, phototaxis receptor, signaling protein
Biological sourceNatronomonas pharaonis
Cellular locationCell membrane; Multi-pass membrane protein: P42196
Total number of polymer chains1
Total formula weight23752.28
Authors
Luecke, H. (deposition date: 2001-06-25, release date: 2001-07-18, Last modification date: 2024-10-16)
Primary citationLuecke, H.,Schobert, B.,Lanyi, J.K.,Spudich, E.N.,Spudich, J.L.
Crystal structure of sensory rhodopsin II at 2.4 angstroms: insights into color tuning and transducer interaction.
Science, 293:1499-1503, 2001
Cited by
PubMed Abstract: We report an atomic-resolution structure for a sensory member of the microbial rhodopsin family, the phototaxis receptor sensory rhodopsin II (NpSRII), which mediates blue-light avoidance by the haloarchaeon Natronobacterium pharaonis. The 2.4 angstrom structure reveals features responsible for the 70- to 80-nanometer blue shift of its absorption maximum relative to those of haloarchaeal transport rhodopsins, as well as structural differences due to its sensory, as opposed to transport, function. Multiple factors appear to account for the spectral tuning difference with respect to bacteriorhodopsin: (i) repositioning of the guanidinium group of arginine 72, a residue that interacts with the counterion to the retinylidene protonated Schiff base; (ii) rearrangement of the protein near the retinal ring; and (iii) changes in tilt and slant of the retinal polyene chain. Inspection of the surface topography reveals an exposed polar residue, tyrosine 199, not present in bacteriorhodopsin, in the middle of the membrane bilayer. We propose that this residue interacts with the adjacent helices of the cognate NpSRII transducer NpHtrII.
PubMed: 11452084
DOI: 10.1126/science.1062977
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

227111

數據於2024-11-06公開中

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