1f50

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|PDB= 1f50 |SIZE=350|CAPTION= <scene name='initialview01'>1f50</scene>, resolution 1.70&Aring;
|PDB= 1f50 |SIZE=350|CAPTION= <scene name='initialview01'>1f50</scene>, resolution 1.70&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=LI1:1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL'>LI1</scene>, <scene name='pdbligand=SQU:2,10,23-TRIMETHYL-TETRACOSANE'>SQU</scene> and <scene name='pdbligand=RET:RETINAL'>RET</scene>
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|LIGAND= <scene name='pdbligand=LI1:1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL'>LI1</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene>, <scene name='pdbligand=SQU:2,10,23-TRIMETHYL-TETRACOSANE'>SQU</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1c3w|1C3W]], [[1c8r|1C8R]], [[1c8s|1C8S]], [[1f4z|1F4Z]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f50 OCA], [http://www.ebi.ac.uk/pdbsum/1f50 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f50 RCSB]</span>
}}
}}
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[[Category: Rosengarth, A.]]
[[Category: Rosengarth, A.]]
[[Category: Schobert, B.]]
[[Category: Schobert, B.]]
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[[Category: LI1]]
 
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[[Category: RET]]
 
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[[Category: SQU]]
 
[[Category: 7-transmembrane]]
[[Category: 7-transmembrane]]
[[Category: e204q mutant ground state]]
[[Category: e204q mutant ground state]]
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[[Category: retinal protein]]
[[Category: retinal protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:04:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:16:04 2008''

Revision as of 17:16, 30 March 2008

Image:1f50.jpg


PDB ID 1f50

Drag the structure with the mouse to rotate
, resolution 1.70Å
Ligands: , ,
Related: 1C3W, 1C8R, 1C8S, 1F4Z


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



BACTERIORHODOPSIN-BR STATE OF THE E204Q MUTANT AT 1.7 ANGSTROM RESOLUTION


Overview

In order to understand how isomerization of the retinal drives unidirectional transmembrane ion transport in bacteriorhodopsin, we determined the atomic structures of the BR state and M photointermediate of the E204Q mutant, to 1.7 and 1.8 A resolution, respectively. Comparison of this M, in which proton release to the extracellular surface is blocked, with the previously determined M in the D96N mutant indicates that the changes in the extracellular region are initiated by changes in the electrostatic interactions of the retinal Schiff base with Asp85 and Asp212, but those on the cytoplasmic side originate from steric conflict of the 13-methyl retinal group with Trp182 and distortion of the pi-bulge of helix G. The structural changes suggest that protonation of Asp85 initiates a cascade of atomic displacements in the extracellular region that cause release of a proton to the surface. The progressive relaxation of the strained 13-cis retinal chain with deprotonated Schiff base, in turn, initiates atomic displacements in the cytoplasmic region that cause the intercalation of a hydrogen-bonded water molecule between Thr46 and Asp96. This accounts for the lowering of the pK(a) of Asp96, which then reprotonates the Schiff base via a newly formed chain of water molecules that is extending toward the Schiff base.

About this Structure

1F50 is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.

Reference

Coupling photoisomerization of retinal to directional transport in bacteriorhodopsin., Luecke H, Schobert B, Cartailler JP, Richter HT, Rosengarth A, Needleman R, Lanyi JK, J Mol Biol. 2000 Jul 28;300(5):1237-55. PMID:10903866

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