1RZ2
1.6A crystal structure of the protein BA4783/Q81L49 (similar to sortase B) from Bacillus anthracis.
Summary for 1RZ2
| Entry DOI | 10.2210/pdb1rz2/pdb |
| Related | 1NG5 |
| Descriptor | conserved hypothetical protein BA4783 (2 entities in total) |
| Functional Keywords | sortase b protein, b. anthracis, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function |
| Biological source | Bacillus anthracis |
| Total number of polymer chains | 1 |
| Total formula weight | 30144.94 |
| Authors | Wu, R.,Zhang, R.,Gornicki, P.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2003-12-23, release date: 2004-07-06, Last modification date: 2024-02-14) |
| 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 Cited by 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: 15242591DOI: 10.1016/j.str.2004.06.001 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
Download full validation report
