4L35

Crystal structure of cruxrhodopsin-3 at pH5 from Haloarcula vallismortis at 2.1 angstrom resolution

Summary for 4L35

• Entry DOI: 10.2210/pdb4l35/pdb
• Related: 1iw6 4JR8
• Descriptor: Cruxrhodopsin-3, RETINAL, BACTERIORUBERIN, ... (4 entities in total)
• Functional Keywords: protein-bacterioruberin complex, seven transmembrane alpha helices, light-driven proton pump, membrane, proton transport
• Biological source: Haloarcula vallismortis
• Cellular location: Cell membrane; Multi-pass membrane protein: P94854
• Total number of polymer chains: 1
• Total formula weight: 27892.80

Authors

Kouyama, T.,Chan, S.K. (deposition date: 2013-06-05, release date: 2014-06-11, Last modification date: 2024-10-30)

Primary citation

Chan, S.K.,Kitajima-Ihara, T.,Fujii, R.,Gotoh, T.,Murakami, M.,Ihara, K.,Kouyama, T.
Crystal structure of Cruxrhodopsin-3 from Haloarcula vallismortis
Plos One, 9:e108362-e108362, 2014

PubMed Abstract: Cruxrhodopsin-3 (cR3), a retinylidene protein found in the claret membrane of Haloarcula vallismortis, functions as a light-driven proton pump. In this study, the membrane fusion method was applied to crystallize cR3 into a crystal belonging to space group P321. Diffraction data at 2.1 Å resolution show that cR3 forms a trimeric assembly with bacterioruberin bound to the crevice between neighboring subunits. Although the structure of the proton-release pathway is conserved among proton-pumping archaeal rhodopsins, cR3 possesses the following peculiar structural features: 1) The DE loop is long enough to interact with a neighboring subunit, strengthening the trimeric assembly; 2) Three positive charges are distributed at the cytoplasmic end of helix F, affecting the higher order structure of cR3; 3) The cytoplasmic vicinity of retinal is more rigid in cR3 than in bacteriorhodopsin, affecting the early reaction step in the proton-pumping cycle; 4) the cytoplasmic part of helix E is greatly bent, influencing the proton uptake process. Meanwhile, it was observed that the photobleaching of retinal, which scarcely occurred in the membrane state, became significant when the trimeric assembly of cR3 was dissociated into monomers in the presence of an excess amount of detergent. On the basis of these observations, we discuss structural factors affecting the photostabilities of ion-pumping rhodopsins.

PubMed: 25268964
DOI: 10.1371/journal.pone.0108362

Experimental method

X-RAY DIFFRACTION (2.1 Å)