Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein fromMycobacterium tuberculosis

Biopolymers ◽  
2014 ◽  
Vol 101 (7) ◽  
pp. 712-719 ◽  
Author(s):  
Luisa Calvanese ◽  
Lucia Falcigno ◽  
Cira Maglione ◽  
Daniela Marasco ◽  
Alessia Ruggiero ◽  
...  
Keyword(s):  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Binding Properties ◽  
Pasta Domain

scholarly journals Interaction of Penicillin-Binding Protein 2 with Soluble Lytic Transglycosylase B1 in Pseudomonas aeruginosa

2008 ◽  
Vol 190 (20) ◽  
pp. 6922-6926 ◽  
Author(s):  
Blaine A. Legaree ◽  
Anthony J. Clarke
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Membrane Protein ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Binding Properties ◽  
Binding Partner ◽  
Lytic Transglycosylase ◽  
Interaction Partners

ABSTRACT Soluble lytic transglycosylase B1 from Pseudomonas aeruginosa was coupled to Sepharose and used to immobilize interaction partners from membrane protein extracts. Penicillin-binding protein 2 (PBP2) was identified as a binding partner, suggesting that the two proteins function together in the biosynthesis of peptidoglycan. By use of an engineered truncated derivative, the N-terminal module of PBP2 was found to confer the binding properties.

scholarly journals PenA, a penicillin-binding protein-type thioesterase specialized for small peptide cyclization

2021 ◽  
Author(s):  
Kenichi Matsuda ◽  
Kei Fujita ◽  
Toshiyuki Wakimoto
Keyword(s):  
Enzymatic Activity ◽  
Computational Model ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Small Peptide ◽  
Peptide Cyclization ◽  
Chain Lengths ◽  
Non Ribosomal Peptides

Abstract Penicillin binding protein-type thioesterases (PBP-type TEs) are a recently identified group of peptide cyclases that catalyze head-to-tail macrolactamization of non-ribosomal peptides. PenA, a new member of this group, is involved in the biosyntheses of cyclic pentapeptides. In this study, we demonstrated the enzymatic activity of PenA in vitro, and analyzed its substrate scope with a series of synthetic substrates. A comparison of the reaction profiles between PenA and SurE, a representative PBP-type TE, showed that PenA is more specialized for small peptide cyclization. A computational model provided a possible structural rationale for the altered specificity for substrate chain lengths.

Sign in / Sign up

Export Citation Format

Share Document