Halobacteria H.sp.xz 515 was isolated from a salt lake in Tibet. Although proton release-and-uptake across claret membrane is in reverse order compared to bacteri-orhodopsin in purple membrane from Halobacterium Sali-...Halobacteria H.sp.xz 515 was isolated from a salt lake in Tibet. Although proton release-and-uptake across claret membrane is in reverse order compared to bacteri-orhodopsin in purple membrane from Halobacterium Sali-narum, and its efficiency of proton pump is much lower, AFM image shows that the molecules are still arranged in a two-dimensional hexagonal lattice of trimers. Primary structure of C- to G-helix of the archaerhodopsin shows that it has only 56% homology with bacteriorhodopsin. But the interactive amino acid residues at the interface between B-and D-helixes are conserved. These amino acid residues are believed to play a significant role in the stability of protein oligomers.展开更多
基金This work was supported by the National Natural Science Foundation of China (Grant Nos. 19890385, 39730150 and 19725415) the key programs of the Chinese Academy of Sciences (Grant Nos.KJ951-A1-603, KJ951-A1-409, KJ952-J1-469 and STZ-00-07).
文摘Halobacteria H.sp.xz 515 was isolated from a salt lake in Tibet. Although proton release-and-uptake across claret membrane is in reverse order compared to bacteri-orhodopsin in purple membrane from Halobacterium Sali-narum, and its efficiency of proton pump is much lower, AFM image shows that the molecules are still arranged in a two-dimensional hexagonal lattice of trimers. Primary structure of C- to G-helix of the archaerhodopsin shows that it has only 56% homology with bacteriorhodopsin. But the interactive amino acid residues at the interface between B-and D-helixes are conserved. These amino acid residues are believed to play a significant role in the stability of protein oligomers.
