3WQJ

Crystal structure of archaerhodopsin-2 at 1.8 angstrom resolution

Summary for 3WQJ

• Entry DOI: 10.2210/pdb3wqj/pdb
• Related: 1iw6 1uaz 1vgo 2EI4 2Z55 4FBZ
• Descriptor: Archaerhodopsin-2, RETINAL, BACTERIORUBERIN, ... (9 entities in total)
• Functional Keywords: 7 trans-membrane helices, light-driven proton pump, transport protein
• Biological source: Halobacterium
• Total number of polymer chains: 1
• Total formula weight: 32638.67

Authors

Kouyama, T. (deposition date: 2014-01-27, release date: 2014-10-15, Last modification date: 2023-11-08)

Primary citation

Kouyama, T.,Fujii, R.,Kanada, S.,Nakanishi, T.,Chan, S.K.,Murakami, M.
Structure of archaerhodopsin-2 at 1.8 angstrom resolution.
Acta Crystallogr.,Sect.D, 70:2692-2701, 2014

PubMed Abstract: Archaerhodopsin-2 (aR2), the sole protein found in the claret membrane of Halorubrum sp. Aus-2, functions as a light-driven proton pump. In this study, structural analysis of aR2 was performed using a novel three-dimensional crystal prepared by the successive fusion of claret membranes. The crystal is made up of stacked membranes, in each of which aR2 trimers are arranged on a hexagonal lattice. This lattice structure resembles that found in the purple membrane of H. salinarum, except that lipid molecules trapped within the trimeric structure are not distributed with perfect threefold symmetry. Nonetheless, diffraction data at 1.8 Å resolution provide accurate structural information about functionally important residues. It is shown that two glutamates in the proton-release channel form a paired structure that is maintained by a low-barrier hydrogen bond. Although the structure of the proton-release pathway is highly conserved among proton-pumping archaeal rhodopsins, aR2 possesses the following peculiar structural features: (i) the motional freedom of the tryptophan residue that makes contact with the C13 methyl group of retinal is restricted, affecting the formation/decay kinetics of the L state, and (ii) the N-terminal polypeptide folds into an Ω-loop, which may play a role in organizing the higher-order structure.

PubMed: 25286853
DOI: 10.1107/S1399004714017313

Experimental method

X-RAY DIFFRACTION (1.8 Å)