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Acta Crystallogr F Struct Biol Commun ; 72(Pt 12): 863-869, 2016 12 01.
Article in English | MEDLINE | ID: mdl-27917833

ABSTRACT

The structure of Msmeg_6760, a protein of unknown function, has been determined. Biochemical and bioinformatics analyses determined that Msmeg_6760 interacts with a protein encoded in the same operon, Msmeg_6762, and predicted that the operon is a toxin-antitoxin (TA) system. Structural comparison of Msmeg_6760 with proteins of known function suggests that Msmeg_6760 binds a hydrophobic ligand in a buried cavity lined by large hydrophobic residues. Access to this cavity could be controlled by a gate-latch mechanism. The function of the Msmeg_6760 toxin is unknown, but structure-based predictions revealed that Msmeg_6760 and Msmeg_6762 are homologous to Rv2034 and Rv2035, a predicted novel TA system involved in Mycobacterium tuberculosis latency during macrophage infection. The Msmeg_6760 toxin fold has not been previously described for bacterial toxins and its unique structural features suggest that toxin activation is likely to be mediated by a novel mechanism.


Subject(s)
Antitoxins/chemistry , Bacterial Toxins/chemistry , Gene Expression Regulation, Bacterial , Mycobacterium smegmatis/chemistry , Toxin-Antitoxin Systems/genetics , Amino Acid Sequence , Antigens, Bacterial , Antitoxins/genetics , Antitoxins/metabolism , Bacterial Proteins , Bacterial Toxins/genetics , Bacterial Toxins/metabolism , Binding Sites , Cloning, Molecular , Crystallography, X-Ray , Escherichia coli/genetics , Escherichia coli/metabolism , Gene Expression , Models, Molecular , Mycobacterium smegmatis/genetics , Mycobacterium smegmatis/metabolism , Mycobacterium tuberculosis/chemistry , Mycobacterium tuberculosis/genetics , Mycobacterium tuberculosis/metabolism , Operon , Plasmids/chemistry , Plasmids/metabolism , Protein Binding , Protein Conformation, alpha-Helical , Protein Conformation, beta-Strand , Protein Interaction Domains and Motifs , Recombinant Proteins/chemistry , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Repressor Proteins
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