The C‐terminal domain of Corynebacterium glutamicum mycoloyltransferase A is composed of five repeated motifs involved in cell wall binding and stability

Abstract

Bacterial cell envelopes are essential complex structures involved in morphology, resistance to environmental stress, signal transduction and transport of solutes and macromolecules. These basic physiological functions are assumed by cell envelope proteins, which can include adhesins and virulence factors in the case of pathogenic species. Proteins present in bacterial cell envelopes are either directly associated with the membranes, for example, transmembrane proteins and lipoproteins, or bound to specific polysaccharidic components of the cell wall, including peptidoglycan (PGN) and cell wall secondary polymers (CWSPs). For instance, many proteins of monoderm Gram-positive bacteria are covalently linked to the PGN by a transpeptidation reaction, which is catalyzed by enzymes

Bioinformatic characterization of endolysins and holin-like membrane proteins in the lysis cassette of phages that infect Gordonia rubripertincta

“…These findings are consistent with the work in mycobacteriophages that also found the Ami-2 domain to be the most prominent [ 22 ]. In addition, domains were identified in the Gordonia phage LysA proteins that folded with high probability and low e values to several PDBs with predicted C-terminal cell wall binding domains (CW1 and CW2) [ 60 , 61 ] or had less defined enzymatic activity (GS25?). However, unlike the mycobacteriophages where the C-terminal cell wall binding domains were identified in a high number of LysA proteins, only 6 of the 16 Gordonia phages had defined CW binding regions through HHpred analysis.…”

Proteomic Analysis of the Mycobacterium tuberculosis Outer Membrane for Potential Implications in Uptake of Small Molecules

“…The outer membrane of mycobacteria has been a formidable barrier for molecules; therefore, how drugs and other molecules traverse through it is still an enigma. As we learn more about the nature and composition of the mycomembrane, ,, it is important to characterize the outer membrane proteome and investigate the role of the OMPs in the uptake of hydrophilic molecules in M. tuberculosis.…”

“…21 The outer membrane of mycobacteria has been a formidable barrier for molecules; therefore, how drugs and other molecules traverse through it is still an enigma. As we learn more about the nature and composition of the mycomembrane, 7,60,61 it is important to characterize the outer membrane proteome and investigate the role of the OMPs in the uptake of hydrophilic molecules in M. tuberculosis. Knowledge about the structure and the biophysical properties of OMPs would aid in elucidating their role in drug uptake and developing effective strategies to improve the permeation of drugs, which can increase the efficacy of the new and existing drugs.…”

Outer membrane proteins inMycobacterium tuberculosisand its potential role in small molecule permeation

“…The outer membrane of Mycobacteria has been an almost impenetrable barrier for molecules therefore how drugs and other molecules traverse through it is still an enigma. As we learn more about the nature and composition of mycomembrane (6,76,77), it is important to characterize the outer membrane proteome and investigate the role of the OMPs in uptake of hydrophilic molecules in M. tuberculosis . Identifying the pore forming proteins is a crucial step in understanding the cell envelope permeability in slow-growing mycobacteria.…”