1NG5

2.0 A crystal structure of Staphylococcus aureus Sortase B

Summary for 1NG5

• Entry DOI: 10.2210/pdb1ng5/pdb
• Descriptor: sortase B (2 entities in total)
• Functional Keywords: structural genomics, a new fold, psi, protein structure initiative, midwest center for structural genomics, mcsg, hydrolase, transferase
• Biological source: Staphylococcus aureus subsp. aureus
• Total number of polymer chains: 2
• Total formula weight: 51282.00

Authors

Zhang, R.,Joachimiak, G.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2002-12-16, release date: 2003-09-23, Last modification date: 2024-05-22)

Primary citation

Zhang, R.,Wu, R.,Joachimiak, G.,Mazmanian, S.K.,Missiakas, D.M.,Gornicki, P.,Schneewind, O.,Joachimiak, A.
Structures of sortase B from Staphylococcus aureus and Bacillus anthracis reveal catalytic amino acid triad in the active site.
Structure, 12:1147-1156, 2004

PubMed Abstract: 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 A 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.

PubMed: 15242591
DOI: 10.1016/j.str.2004.06.001

Experimental method

X-RAY DIFFRACTION (2 Å)