ArticlePloS one2012
Mutational analysis of Cvab, an ABC transporter involved in the secretion of active colicin V.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
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- Antibacterial action, proteolytic immunity, and in vivo activity of a Vibrio cholerae microcin.Cell host & microbe · 2024Article
- Semantic search using protein large language models detects class II microcins in bacterial genomes.mSystems · 2024Article
- Secretion of the human parathyroid hormone through a microcin type I secretion system in Escherichia coli.Microbial cell factories · 2024Article
- Export of Diverse and Bioactive Small Proteins through a Type I Secretion System.Applied and environmental microbiology · 2023Article
- Evidence for Widespread Class II Microcins inApplied and environmental microbiology · 2022Article
- Microcins reveal natural mechanisms of bacterial manipulation to inform therapeutic development.Microbiology (Reading, England) · 2022Article
- Biosynthesis and secretion of the microbial sulfated peptide RaxX and binding to the rice XA21 immune receptor.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Secretome of obligate intracellular Rickettsia.FEMS microbiology reviews · 2015Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
CvaB is the central membrane transporter of the colicin V secretion system that belongs to an ATP-binding cassette superfamily. Previous data showed that the N-terminal and C-terminal domains of CvaB are essential for the function of CvaB. N-terminal domain of CvaB possesses Ca(2+)-dependent cysteine proteolytic activity, and two critical residues, Cys32 and His105, have been identified. In this study, we also identify Asp121 as being the third residue of the putative catalytic triad within the active site of the enzyme. The Asp121 mutants lose both their colicin V secretion activity and N-terminal proteolytic activity. The adjacent residue Pro122 also appears to play a critical role in the colicin V secretion. However, the reversal of the two residues D121P - P122D results in loss of activity. Based on molecular modeling and protein sequence alignment, several residues adjacent to the critical residues, Cys32 and His105, were also examined and characterized. Site-directed mutagenesis of Trp101, Asp102, Val108, Leu76, Gly77, and Gln26 indicate that the neighboring residues around the catalytic triad affect colicin V secretion. Several mutated CvaB proteins with defective secretion were also tested, including Asp121 and Pro122, and were found to be structurally stable. These results indicate that the residues surrounding the identified catalytic triad are functionally involved in the secretion of biologically active colicin V.
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