Journal
STRUCTURE
Volume 12, Issue 7, Pages 1147-1156Publisher
CELL PRESS
DOI: 10.1016/j.str.2004.06.001
Keywords
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Funding
- NIAID NIH HHS [R01 AI038897, AI38897, R01 AI052474, 1U54 AI 057153, AI 52474, U54 AI057153] Funding Source: Medline
- NIGMS NIH HHS [GM 62414, P50 GM062414, R01 GM058266, P50 GM062414-02, GM 58266] Funding Source: Medline
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Surface proteins attached by sortases to the cell wall envelope of bacterial pathogens play important roles during infection. Sorting and attachment of these proteins is directed by C-terminal signals. Sortase B of S. aureus recognizes a motif NPQTN, cleaves the polypeptide after the Thr residue, and attaches the protein to pentaglycine cross-bridges. Sortase B of B. anthracis is thought to recognize the NPKTG motif, and attaches surface proteins to m-diaminopimelic acid cross-bridges. We have determined crystal structure of sortase B from B. anthracis and S. aureus at 1.6 and 2.0 Angstrom resolutions, respectively. These structures show a beta-barrel fold with alpha-helical elements on its outside, a structure thus far exclusive to the sortase family. A putative active site located on the edge of the beta-barrel is comprised of a Cys-His-Asp catalytic triad and presumably faces the bacterial cell surface. A putative binding site for the sorting signal is located nearby.
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