| Mycobacterial PE_PGRS Proteins Contain Calcium-Binding Motifs with Parallel β-roll Folds |
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| 作者单位： | Nandita Bachhawat（Department of Bioinformatics, DAV College, Chandigarh 160012, India） ;
Balvinder Singh（Institute of Microbial Technology,Chandigarh 160036, India） ; |
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| 摘 要： | The PE_PGRS family of proteins unique to mycobacteria is demonstrated to con- rain multiple calcium-binding and glycine-rich sequence motifs GGXGXD/NXUX. This sequence repeat constitutes a calcium-binding parallel/3-roll or parallel β-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 Ught of macrophage-pathogen interaction and pathogenesis is presented.
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| 关 键 词： | 肺结核 度性因素 基序 钙元素 支原体病菌 |
Mycobacterial PE_PGRS Proteins Contain Calcium-Binding Motifs with Parallel β-roll Folds |
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| Authors: | Nandita Bachhawat Balvinder Singh |
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| Institution: | [1]G.N. Ramachandran Knowledge Center for Genome Informatics, Institute of Genomics and Integrative Biology, Council of Scientific and Industrial Research, Delhi 110007, India [2]Institute of Microbial Technology, Chandigarh 160036, India |
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| Abstract: | The PE_PGRS family of proteins unique to mycobacteria is demonstrated to con- rain multiple calcium-binding and glycine-rich sequence motifs GGXGXD/NXUX. This sequence repeat constitutes a calcium-binding parallel/3-roll or parallel β-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 Ught of macrophage-pathogen interaction and pathogenesis is presented. |
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