Abstract
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 Å resolution. The observed structural rearrangements were localized near the retinal chromophore, with a key water molecule becoming disordered and the retinal's β-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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 473-482 |
| Number of pages | 10 |
| Journal | Structure |
| Volume | 10 |
| Issue number | 4 |
| DOIs | |
| State | Published - 2002 |
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Keywords
- Archael rhodopsins
- Kinetic crystallography
- Sensory rhodopsin II
- Signal transduction
- Structural intermediates
- Structural mechanism
ASJC Scopus subject areas
- Molecular Biology
- Structural Biology
Cite this
Early structural rearrangements in the photocycle of an integral membrane sensory receptor. / Edman, Karl; Royant, Antoine; Nollert, Peter; Maxwell, Carrie A.; Pebay-Peyroula, Eva; Navarro, Javier; Neutze, Richard; Landau, Ehud M.
In: Structure, Vol. 10, No. 4, 2002, p. 473-482.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Early structural rearrangements in the photocycle of an integral membrane sensory receptor
AU - Edman, Karl
AU - Royant, Antoine
AU - Nollert, Peter
AU - Maxwell, Carrie A.
AU - Pebay-Peyroula, Eva
AU - Navarro, Javier
AU - Neutze, Richard
AU - Landau, Ehud M.
PY - 2002
Y1 - 2002
N2 - 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 Å resolution. The observed structural rearrangements were localized near the retinal chromophore, with a key water molecule becoming disordered and the retinal's β-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.
AB - 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 Å resolution. The observed structural rearrangements were localized near the retinal chromophore, with a key water molecule becoming disordered and the retinal's β-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.
KW - Archael rhodopsins
KW - Kinetic crystallography
KW - Sensory rhodopsin II
KW - Signal transduction
KW - Structural intermediates
KW - Structural mechanism
UR - http://www.scopus.com/inward/record.url?scp=0036230849&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036230849&partnerID=8YFLogxK
U2 - 10.1016/S0969-2126(02)00736-0
DO - 10.1016/S0969-2126(02)00736-0
M3 - Article
C2 - 11937052
AN - SCOPUS:0036230849
VL - 10
SP - 473
EP - 482
JO - Structure with Folding & design
JF - Structure with Folding & design
SN - 0969-2126
IS - 4
ER -