2i21
From Proteopedia
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|PDB= 2i21 |SIZE=350|CAPTION= <scene name='initialview01'>2i21</scene>, resolution 1.84Å | |PDB= 2i21 |SIZE=350|CAPTION= <scene name='initialview01'>2i21</scene>, resolution 1.84Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |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= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i21 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i21 OCA], [http://www.ebi.ac.uk/pdbsum/2i21 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i21 RCSB]</span> | ||
}} | }} | ||
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[[Category: Lanyi, J K.]] | [[Category: Lanyi, J K.]] | ||
[[Category: Schobert, B.]] | [[Category: Schobert, B.]] | ||
| - | [[Category: LI1]] | ||
| - | [[Category: RET]] | ||
| - | [[Category: SQU]] | ||
[[Category: 7-transmembrane]] | [[Category: 7-transmembrane]] | ||
[[Category: haloarchaea]] | [[Category: haloarchaea]] | ||
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[[Category: serpentine]] | [[Category: serpentine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:38:39 2008'' |
Revision as of 00:38, 31 March 2008
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| , resolution 1.84Å | |||||||
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| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Bacteriorhodopsin/lipid complex, T46V mutant
Overview
The X-ray diffraction structure of the non-illuminated D96A bacteriorhodopsin mutant reveals structural changes as far away as 15 A from residue 96, at the retinal, Trp-182, Ala-215, and waters 501, 402, and 401. The Asp-to-Ala side-chain replacement breaks its hydrogen bond with Thr-46, and the resulting separation of the cytoplasmic ends of helices B and C is communicated to the retinal region through a chain of covalent and hydrogen bonds. The unexpected long-range consequences of the D96A mutation include breaking the hydrogen bond between O of Ala-215 and water 501 and the formation of a new hydrogen bond between water molecules 401 and 402 in the extracellular region. Because in the T46V mutant a new water molecule appears at Asp-96 and its hydrogen-bond to Ile-45 replaces Thr-46 as its link to helix B, the separation of helices B and C is smaller than that in D96A, and there are no atomic displacements elsewhere in the protein. Propagation of conformational changes along the chain between the retinal and Thr-46 had been observed earlier in the crystal structures of the D96N and E204Q mutants but in the trapped M state. Consistent with the perturbation of the retinal region in D96A, little change of the Thr-46 region occurs between the non-illuminated and M states of this mutant. It appears that a local perturbation can propagate along a track in both directions between the retinal and the Asp-96/Thr-46 pair, either from photoisomerization of the retinal in the wild-type protein in one case or from the D96A mutation in the other.
About this Structure
2I21 is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.
Reference
Propagating structural perturbation inside bacteriorhodopsin: crystal structures of the M state and the D96A and T46V mutants., Lanyi JK, Schobert B, Biochemistry. 2006 Oct 3;45(39):12003-10. PMID:17002299
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