Related Experiment Video
Updated: Jul 7, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
Published on: May 13, 2020
Mycobacterial PE_PGRS proteins contain calcium-binding motifs with parallel beta-roll folds
Nandita Bachhawat1, Balvinder Singh
1G.N. Ramachandran Knowledge Center for Genome Informatics, Institute of Genomics and Integrative Biology, Council of Scientific and Industrial Research, Delhi 110007, India. nanditabachhawat45@gmail.com
Abstract:
The PE_PGRS family of proteins unique to mycobacteria is demonstrated to contain multiple calcium-binding and glycine-rich sequence motifs GGXGXD/NXUX. This sequence repeat constitutes a calcium-binding parallel beta-roll or parallel beta-helix structure and is found in RTX toxins secreted by many Gram-negative bacteria. It is predicted that the highly homologous PE PGRS proteins containing multiple copies of the nona-peptide motif could fold into similar calcium-binding structures. The implication of the predicted calcium-binding property of PE PGRS proteins in the light of macrophage-pathogen interaction and pathogenesis is presented.
More Related Videos
Related Concept Videos
Multi-pass Transmembrane Proteins and β-barrels
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Calmodulin-dependent Signaling
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Cytoskeletal Proteins in Bacteria
Structure of Porins
Bacterial Protein Maturation
Bacterial Phylum Actinobacteria

