5O8X

The X-ray Structure of Catenated Lytic Transglycosylase SltB1 from Pseudomonas aeruginosa

Summary for 5O8X

• Entry DOI: 10.2210/pdb5o8x/pdb
• Descriptor: Soluble lytic transglycosylase B, CALCIUM ION, CACODYLATE ION, ... (5 entities in total)
• Functional Keywords: lytic transglycosylase, lyase
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 2
• Total formula weight: 69387.52

Authors

Dominguez-Gil, T.,Molina, R. (deposition date: 2017-06-14, release date: 2017-11-29, Last modification date: 2024-05-08)

Primary citation

Dominguez-Gil, T.,Molina, R.,Dik, D.A.,Spink, E.,Mobashery, S.,Hermoso, J.A.
X-ray Structure of Catenated Lytic Transglycosylase SltB1.
Biochemistry, 56:6317-6320, 2017

PubMed 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.

PubMed: 29131935
DOI: 10.1021/acs.biochem.7b00932

Experimental method

X-RAY DIFFRACTION (2.5 Å)