4G29

Structure of the Catalytic Domain of the Salmonella Virulence Factor SseI

Summary for 4G29

• Entry DOI: 10.2210/pdb4g29/pdb
• Related: 4G2B
• Descriptor: Secreted effector protein sseI (2 entities in total)
• Functional Keywords: cysteine protease superfamily, protein binding
• Biological source: Salmonella enterica subsp. enterica serovar Typhimurium
• Cellular location: Secreted: Q8ZQ79
• Total number of polymer chains: 1
• Total formula weight: 21655.41

Authors

Stebbins, C.E.,Bhaskaran, S.S. (deposition date: 2012-07-11, release date: 2012-11-28, Last modification date: 2024-11-20)

Primary citation

Bhaskaran, S.S.,Stebbins, C.E.
Structure of the catalytic domain of the Salmonella virulence factor SseI.
Acta Crystallogr.,Sect.D, 68:1613-1621, 2012

PubMed Abstract: 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.

PubMed: 23151626
DOI: 10.1107/S0907444912039042

Experimental method

X-RAY DIFFRACTION (1.7 Å)