Structure of the catalytic domain of theSalmonellavirulence factor SseI
| Autor: | Bhaskaran Shyam S, C.E. Stebbins |
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| Rok vydání: | 2012 |
| Předmět: |
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Molecular Salmonella bacterial pathogenesis Protein Conformation Virulence Factors Molecular Sequence Data Virulence Biology medicine.disease_cause cysteine proteases Virulence factor Microbiology 03 medical and health sciences Protein structure SrfH type III secretion Structural Biology Catalytic Domain Catalytic triad Hydrolase medicine Amino Acid Sequence Cloning Molecular Peptide sequence 030304 developmental biology 0303 health sciences 030302 biochemistry & molecular biology General Medicine Research Papers SPI-2 Cysteine protease Biochemistry SseI Proteolysis Crystallization |
| Zdroj: | Acta Crystallographica Section D: Biological Crystallography |
| ISSN: | 0907-4449 |
| DOI: | 10.1107/s0907444912039042 |
| Popis: | The C-terminal domain of the Salmonella virulence factor SseI is structurally similar to the cysteine protease superfamily and contains the conserved catalytic triad characteristic of members of this family. SseI is secreted into host cells by Salmonella and contributes to the establishment of systemic infections. The crystal structure of the C-terminal domain of SseI has been solved to 1.70 Å resolution, revealing it to be a member of the cysteine protease superfamily with a catalytic triad consisting of Cys178, His216 and Asp231 that is critical to its virulence activities. Structure-based analysis revealed that SseI is likely to possess either acyl hydrolase or acyltransferase activity, placing this virulence factor in the rapidly growing class of enzymes of this family utilized by bacterial pathogens inside eukaryotic cells. |
| Databáze: | OpenAIRE |
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