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  Three-dimensional structure of the surface protein of Desulfurococcus mobilis

Wildhaber, I., Santarius, U., & Baumeister, W. (1987). Three-dimensional structure of the surface protein of Desulfurococcus mobilis. Journal of Bacteriology., 169(12), 5563-5568.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-74DE-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-74DF-9
Genre: Journal Article

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 Creators:
Wildhaber, I., Author
Santarius, U.1, Author              
Baumeister, W.1, Author              
Affiliations:
1External Organizations, ou_persistent22              

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Free keywords: Archaea/an [Analysis]; *Archaea/ul [Ultrastructure]; *Bacteria/ul [Ultrastructure]; *Bacterial Proteins/an [Analysis]; Cell Membrane/an [Analysis]; Cell Membrane/ul [Ultrastructure]; Freeze Etching; Image Processing, Computer-Assisted; *Membrane Proteins/an [Analysis]; Microscopy, Electron
 Abstract: The spherical cells of the thermophilic, sulfur-dependent archaebacterium Desulfurococcus mobilis are completely covered with a relatively poorly ordered, tetragonally arrayed surface protein. The structure of this surface protein was examined by using three-dimensional electron microscopy. The protein lattice forms an open meshwork composed of cross-shaped morphological units, which are released when glycerol is added. These subunits make contact at the distal ends of their four arms. The p4 symmetry requires that each of these morphological subunits represents a tetramer. The strong interaction of the monomers within the crosses and the relatively weak interaction of the intersecting arms of the crosses within the lattice structure suggest that the tetramers are assembled before their incorporation into the lattice.

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 Dates: 1987
 Publication Status: Published in print
 Pages: -
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 Rev. Type: -
 Identifiers: eDoc: 318347
 Degree: -

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Title: Journal of Bacteriology.
Source Genre: Journal
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Pages: - Volume / Issue: 169 (12) Sequence Number: - Start / End Page: 5563 - 5568 Identifier: -