1IJA
Structure of Sortase
Summary for 1IJA
| Entry DOI | 10.2210/pdb1ija/pdb |
| NMR Information | BMRB: 4879 |
| Descriptor | Sortase (1 entity in total) |
| Functional Keywords | eight stranded beta barrel, transpeptidase, protein binding |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 1 |
| Total formula weight | 16753.00 |
| Authors | Ilangovan, U.,Ton-That, H.,Iwahara, J.,Schneewind, O.,Clubb, R.T. (deposition date: 2001-04-25, release date: 2001-05-09, Last modification date: 2024-05-01) |
| Primary citation | Ilangovan, U.,Ton-That, H.,Iwahara, J.,Schneewind, O.,Clubb, R.T. Structure of sortase, the transpeptidase that anchors proteins to the cell wall of Staphylococcus aureus. Proc.Natl.Acad.Sci.USA, 98:6056-6061, 2001 Cited by PubMed Abstract: Surface proteins of Gram-positive bacteria play important roles during the pathogenesis of human infections and require sortase for anchoring to the cell-wall envelope. Sortase cleaves surface proteins at the LPXTG motif and catalyzes the formation of an amide bond between the carboxyl group of threonine (T) and the amino group of cell-wall crossbridges. The NMR structure of sortase reveals a unique beta-barrel structure, in which the active-site sulfhydryl of cysteine-184 is poised for ionization by histidine-120, presumably enabling the resultant thiolate to attack the LPXTG peptide. Calcium binding near the active site stimulates catalysis, possibly by altering the conformation of a surface loop that recognizes newly translocated polypeptides. The structure suggests a mechanistic relationship to the papain/cathepsin proteases and should facilitate the design of new antiinfective agents. PubMed: 11371637DOI: 10.1073/pnas.101064198 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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