Structure of the light-driven chloride pump halorhodopsin at 1.8 angstrom resolution

Citation
M. Kolbe et al., Structure of the light-driven chloride pump halorhodopsin at 1.8 angstrom resolution, SCIENCE, 288(5470), 2000, pp. 1390-1396
Citations number
47
Categorie Soggetti
Multidisciplinary,Multidisciplinary,Multidisciplinary
Journal title
SCIENCE
ISSN journal
00368075 → ACNP
Volume
288
Issue
5470
Year of publication
2000
Pages
1390 - 1396
Database
ISI
SICI code
0036-8075(20000526)288:5470<1390:SOTLCP>2.0.ZU;2-Y
Abstract
Halorhodopsin, an archaeal rhodopsin ubiquitous in Haloarchaea, uses Light energy to pump chloride through biological membranes. Halorhodopsin crystal s were grown in a cubic Lipidic phase, which allowed the x-ray structure de termination of this anion pump at 1.8 angstrom resolution. Halorhodopsin as sembles to trimers around a central patch consisting of palmitic acid. Next to the protonated Schiff base between Lys(242) and the isomerizable retina l chromophore, a single chloride ion occupies the transport site. Energetic calculations on chloride binding reveal a combination of ion-ion and ion-d ipole interactions for stabilizing the anion 18 angstroms below the membran e surface. ion dragging across the protonated Schiff base explains why chlo ride and proton translocation modes are mechanistically equivalent in archa eal rhodopsins.