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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Amino Acid Motifs
-
Amino Acid Sequence
-
Antigens, Bacterial / chemistry*
-
Antigens, Bacterial / genetics
-
Antigens, Bacterial / metabolism*
-
Bacterial Proteins / chemistry*
-
Bacterial Proteins / genetics
-
Bacterial Proteins / metabolism*
-
Base Sequence
-
Binding Sites / genetics
-
Calcium / metabolism
-
DNA, Bacterial / genetics
-
Membrane Proteins / chemistry*
-
Membrane Proteins / genetics
-
Membrane Proteins / metabolism*
-
Models, Molecular
-
Molecular Sequence Data
-
Mycobacterium tuberculosis / genetics
-
Mycobacterium tuberculosis / metabolism*
-
Protein Structure, Secondary
Substances
-
Antigens, Bacterial
-
Bacterial Proteins
-
DNA, Bacterial
-
Membrane Proteins
-
PE-PGRS protein, Mycobacterium
-
Calcium