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Structure paper

TitleModest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins.
Journal, issue, pagesNature, Vol. 453, Page 1266-1270, Year 2008
Publish dateMar 27, 2008 (structure data deposition date)
AuthorsJoh, N.H. / Min, A. / Faham, S. / Whitelegge, J.P. / Yang, D. / Woods, V.L. / Bowie, J.U.
External linksNature / PubMed:18500332
MethodsX-ray diffraction
Resolution2.31 - 2.7 Å
Structure data

PDB-3coc:
Crystal Structure of D115A mutant of Bacteriorhodopsin
Method: X-RAY DIFFRACTION / Resolution: 2.31 Å

PDB-3cod:
Crystal Structure of T90A/D115A mutant of Bacteriorhodopsin
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-RET:
RETINAL

ChemComp-HOH:
WATER

Source
  • halobacterium salinarum (Halophile)
KeywordsPROTON TRANSPORT / membrane protein / membrane protein folding / hydrogen bond / Chromophore / Hydrogen ion transport / Ion transport / Photoreceptor protein / Pyrrolidone carboxylic acid / Receptor / Retinal protein / Sensory transduction / Transmembrane / Transport

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