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Molecular analysis of an outer membrane protein, MopB, of Methylococcus capsulatus (Bath) and structural comparisons with proteins of the OmpA family
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UNSPECIFIED (2000) Molecular analysis of an outer membrane protein, MopB, of Methylococcus capsulatus (Bath) and structural comparisons with proteins of the OmpA family. ARCHIVES OF MICROBIOLOGY, 173 (5-6). pp. 346-351. ISSN 0302-8933.
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Abstract
The gene encoding a major outer membrane protein (MopB) of the methanotroph Methylococcus capsulatus (Bath) was cloned and sequenced. The cloned DNA contained an open reading frame of 1044 bp coding for a 348-amino-acid polypeptide with a 21-amino-acid leader peptide. Comparative sequence analysis of the predicted amino acid sequence revealed that the C-terminal part of MopB possessed sequences that are conserved in the OmpA family of proteins. The N-terminal half of the protein had no significant sequence similarity to other proteins in the databases, but the predicted secondary structure showed stretches of amphipathic beta-strands typical of transmembrane segments of outer membrane proteins. A region with four cysteines similar to the cysteine-encompassing region of the OprF of Pseudomonas aeruginosa was found toward the C-terminal part of MopB. Results from whole-cell labeling with the fluorescent thiol-reacting reagent 5-iodoacetamidofluorescein indicated a surface-exposed location for these cysteines. A probe consisting of the 3'-end of the mopB gene hybridized to the type I methanotroph Methylomonas methanica S1 in Southern blots containing DNA from nine methanotrophic strains representing six different genera.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QR Microbiology | ||||
Journal or Publication Title: | ARCHIVES OF MICROBIOLOGY | ||||
Publisher: | SPRINGER VERLAG | ||||
ISSN: | 0302-8933 | ||||
Official Date: | May 2000 | ||||
Dates: |
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Volume: | 173 | ||||
Number: | 5-6 | ||||
Number of Pages: | 6 | ||||
Page Range: | pp. 346-351 | ||||
Publication Status: | Published |
Data sourced from Thomson Reuters' Web of Knowledge
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