2i21: Difference between revisions
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'''Bacteriorhodopsin/lipid complex, T46V mutant''' | '''Bacteriorhodopsin/lipid complex, T46V mutant''' | ||
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[[Category: Schobert, B.]] | [[Category: Schobert, B.]] | ||
[[Category: 7-transmembrane]] | [[Category: 7-transmembrane]] | ||
[[Category: | [[Category: Haloarchaea]] | ||
[[Category: | [[Category: Ion pump]] | ||
[[Category: | [[Category: Ion transport]] | ||
[[Category: | [[Category: Lipid]] | ||
[[Category: | [[Category: Membrane protein]] | ||
[[Category: | [[Category: Photoreceptor]] | ||
[[Category: | [[Category: Retinal protein]] | ||
[[Category: | [[Category: Serpentine]] | ||
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Revision as of 03:59, 4 May 2008
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 Page seeded by OCA on Sun May 4 06:59:04 2008
