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          Institute: MPI für Biochemie     Collection: Structural Biology (W. Baumeister)     Display Documents

ID: 318368.0, MPI für Biochemie / Structural Biology (W. Baumeister)
Tetrabrachion - a filamentous archaebacterial surface protein assembly of unusual structure and extreme stability
Authors:Peters, J.; Nitsch, M.; Kühlmorgen, B.; Golbik, R.; Lupas, A.; Kellermann, J.; Engelhardt, H.; Pfander, J. P.; Müller, S.; Goldie, K.; Engel, A.
Date of Publication (YYYY-MM-DD):1995-01-27
Title of Journal:Journal of Molecular Biology
Issue / Number:4
Start Page:385
End Page:401
Audience:Not Specified
Abstract / Description:The surface (S-) layer of the hyperthermophilic archaebacterium Staphylothermus marinus was isolated, dissected into separate domains by chemical and proteolytic methods, and analyzed by spectroscopic, electron microscopic and biochemical techniques. The S-layer is formed by a poorly ordered meshwork of branched, filiform morphological subunits resembling dandelion seed-heads. A morphological subunit (christened by us tetrabrachion) consists of a 70 nm long, almost perfectly straight stalk ending in four straight arms of 24 nm length that provide lateral connectivity by end-to-end contacts. At 32 nm from the branching point, tetrabrachion carries two globular particles of 10 nm diameter that have both tryptic and chymotryptic protease activity Tetrabrachion is built by a tetramer of M(r) 92,000 polypeptides that form a parallel, four-stranded alpha-helical rod and separate at one end into four strands. These strands interact in a 1:1 stoichiometry with polypeptides of M(r) 85,000 to form the arms. The arms are composed entirely of beta-sheets. All S-layer components contain bound carbohydrates (glucose, mannose, and glucosamine) at a ratio of 38 g/100 g protein for the complete tetrabrachion-protease complex. The unique structure of tetrabrachion is reflected in an extreme thermal stability in the presence of strong denaturants (1% (w/v) SDS of 6M guanidine): the arms, which are stabilized by intramolecular disulphide bridges, melt around 115 degrees C under non-reducing conditions, whereas the stalk sustains heating up to about 130 degrees C. Complete denaturation of the stalk domain requires treatment with 70% (v/v) sulfuric acid or with fuming trifluoromethanesulfonic acid. The globular protease can be heated to 90 degrees C in 6M guanidine and to 120 degrees C in 1% SDS and represents one of the most stable proteases characterized to date. [References: 41]
Free Keywords:S-layer; Archaebacterial; Surface protein; Filamentous thermophilic.; Transmission electron-microscopy; Alpha-fibrous proteins; Helical coiled coils; 3-dimensional structure; Escherichia-coli; Glycoprotein; Laminin; Sequences; Features.; Molecular biology & genetics.
External Publication Status:published
Document Type:Article
Communicated by:Anton Hillebrand
Affiliations:MPI für Biochemie/Structural Biology (W. Baumeister)/
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