PETERS, J and NITSCH, M and KUHLMORGEN, B and GOLBIK, R and LUPAS, A and KELLERMANN, J and ENGELHARDT, H and PFANDER, JP and MULLER, S and GOLDIE, K and ENGEL, A and STETTER, KO and BAUMEISTER, W (1995) TETRABRACHION - A FILAMENTOUS ARCHAEBACTERIAL SURFACE PROTEIN ASSEMBLY OF UNUSUAL STRUCTURE AND EXTREME STABILITY. JOURNAL OF MOLECULAR BIOLOGY, 245 (4). pp. 385-401. ISSN 0022-2836,
Full text not available from this repository.Abstract
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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | TRANSMISSION ELECTRON-MICROSCOPY; ALPHA-FIBROUS PROTEINS; HELICAL COILED COILS; 3-DIMENSIONAL STRUCTURE; S-LAYER; ESCHERICHIA-COLI; GLYCOPROTEIN; LAMININ; SEQUENCES; FEATURES; S-LAYER; ARCHAEBACTERIAL; SURFACE PROTEIN; FILAMENTOUS THERMOPHILIC |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:38 |
| URI: | https://pred.uni-regensburg.de/id/eprint/52787 |
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