1gue: Difference between revisions

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==Overview==

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 .~~.. [[http://ispc.weizmann.ac.il/pmbin/getpm?11937052 (full description)]]~~

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.

==About this Structure==

1GUE is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Natronomonas_pharaonis Natronomonas pharaonis]] with CL and RET as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: RET. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GUE OCA]].

1GUE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Natronomonas_pharaonis Natronomonas pharaonis] with CL and RET as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: RET. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GUE OCA].

==Reference==

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[[Category: phototaxis]]

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on ~~Tue Oct 30 15~~:19:30 2007''

''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:06:24 2007''

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@@ Line 5: / Line 5: @@
 ==Overview==
-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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?11937052 (full description)]]
+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.
 ==About this Structure==
-GUE is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Natronomonas_pharaonis Natronomonas pharaonis]] with CL and RET as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: RET. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GUE OCA]].
+GUE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Natronomonas_pharaonis Natronomonas pharaonis] with CL and RET as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: RET. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GUE OCA].
 ==Reference==
@@ Line 28: / Line 28: @@
 [[Category: phototaxis]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:19:30 2007''
+''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 13:06:24 2007''