Mycobacterial PE_PGRS proteins contain calcium-binding motifs with parallel beta-roll folds.
10.1016/S1672-0229(08)60010-8
- Author:
Nandita BACHHAWAT
1
;
Balvinder SINGH
Author Information
1. G.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
- Publication Type:Journal Article
- MeSH:
Amino Acid Motifs;
Amino Acid Sequence;
Antigens, Bacterial;
chemistry;
genetics;
metabolism;
Bacterial Proteins;
chemistry;
genetics;
metabolism;
Base Sequence;
Binding Sites;
genetics;
Calcium;
metabolism;
DNA, Bacterial;
genetics;
Membrane Proteins;
chemistry;
genetics;
metabolism;
Models, Molecular;
Molecular Sequence Data;
Mycobacterium tuberculosis;
genetics;
metabolism;
Protein Structure, Secondary
- From:
Genomics, Proteomics & Bioinformatics
2007;5(3-4):236-241
- CountryChina
- Language:English
-
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.
