Abstract
Formation of catenanes by proteins is rare, with few known examples. We report herein the X-ray structure of a catenane dimer of lytic transglycosylase SltB1 of Pseudomonas aeruginosa. The enzyme is soluble and exists in the periplasmic space, where it modifies the bacterial cell wall. The catenane dimer exhibits the protein monomers in a noncovalent chain-link arrangement, whereby a stretch of 51 amino acids (to become a loop and three helices) from one monomer threads through the central opening of the structure of the partner monomer. The protein folds after threading in a manner that leaves two helices (α1 and α2) as stoppers to impart stability to the dimer structure. The symmetric embrace by the two SltB1 molecules occludes both active sites entirely, an arrangement that is sustained by six electrostatic interactions between the two monomers. In light of the observation of these structural motifs in all members of Family 3 lytic transglycosylases, catenanes might be present for those enzymes, as well. The dimeric catenane might represent a regulated form of SltB1.
| Original language | English |
|---|---|
| Journal | Biochemistry |
| Volume | 56 |
| Issue number | 48 |
| Pages (from-to) | 6317-6320 |
| Number of pages | 4 |
| ISSN | 0006-2960 |
| DOIs | |
| Publication status | Published - 5 Dec 2017 |
| Externally published | Yes |
Keywords
- Bacterial Proteins/chemistry
- Crystallography, X-Ray
- Models, Molecular
- Peptidoglycan Glycosyltransferase/chemistry
- Protein Conformation
- Protein Folding