Imaging bacteriorhodopsin-like molecules of claret-membranes from Tibet halobacteria xz515 by atomic force microscope

Lin Tang, Qing’an Sun, Qingguo Li, Yibo Huang, QingQing Wei, Yi Zhang, Jun Hu, Zhihong Zhang, Minqian Li, Fujia Yang

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Abstract

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 bacteriorhodopsin in purple membrane from Halobacterium Salinarum, 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.

Original languageEnglish (US)
Pages (from-to)1897-1900
Number of pages4
JournalChinese Science Bulletin
Volume46
Issue number22
DOIs
Publication statusPublished - Jan 1 2001
Externally publishedYes

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Keywords

  • Archaerhodopsin
  • Atomic force microscope
  • Bacteriorhodopsin
  • Halobacteria
  • Hexagonal lattice

ASJC Scopus subject areas

  • General

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