scholarly journals Biochemical and Structural Analysis of a Novel Esterase from Caulobacter crescentus related to Penicillin-Binding Protein (PBP)

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Bum Han Ryu ◽  
Tri Duc Ngo ◽  
Wanki Yoo ◽  
Sojeong Lee ◽  
Boo-Young Kim ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Caulobacter Crescentus ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Novel Esterase

Catalytic Mechanism of theStreptomycesK15dd-Transpeptidase/Penicillin-Binding Protein Probed by Site-Directed Mutagenesis and Structural Analysis†,‡

Biochemistry ◽  
2003 ◽  
Vol 42 (10) ◽  
pp. 2895-2906 ◽  
Author(s):  
Noureddine Rhazi ◽  
Paulette Charlier ◽  
Dominique Dehareng ◽  
Danièle Engher ◽  
Marcel Vermeire ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Catalytic Mechanism ◽  
Binding Protein ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Penicillin Binding Protein

scholarly journals Osmolality-Dependent Relocation of Penicillin-Binding Protein PBP2 to the Division Site in Caulobacter crescentus

2012 ◽  
Vol 194 (12) ◽  
pp. 3116-3127 ◽  
Author(s):  
J. Hocking ◽  
R. Priyadarshini ◽  
C. N. Takacs ◽  
T. Costa ◽  
N. A. Dye ◽  
...  
Keyword(s):  
Caulobacter Crescentus ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Division Site

scholarly journals Caulobacter crescentus Requires RodA and MreB for Stalk Synthesis and Prevention of Ectopic Pole Formation

2005 ◽  
Vol 187 (2) ◽  
pp. 544-553 ◽  
Author(s):  
Jennifer K. Wagner ◽  
Cheryl D. Galvani ◽  
Yves V. Brun
Keyword(s):  
Escherichia Coli ◽  
Cell Body ◽  
Cell Elongation ◽  
Caulobacter Crescentus ◽  
Binding Protein ◽  
Loss Of Control ◽  
Cellular Polarity ◽  
Penicillin Binding Protein ◽  
Body Diameter ◽  
Specialized Form

ABSTRACT Caulobacter crescentus cells treated with amdinocillin, an antibiotic which specifically inhibits the cell elongation transpeptidase penicillin binding protein 2 in Escherichia coli, exhibit defects in stalk elongation and morphology, indicating that stalk synthesis may be a specialized form of cell elongation. In order to investigate this possibility further, we examined the roles of two other proteins important for cell elongation, RodA and MreB. We show that, in C. crescentus, the rodA gene is essential and that RodA depletion leads to a loss of control over stalk and cell body diameter and a stalk elongation defect. In addition, we demonstrate that MreB depletion leads to a stalk elongation defect and conclude that stalk elongation is a more constrained form of cell elongation. Our results strongly suggest that MreB by itself does not determine the diameter of the cell body or stalk. Finally, we show that cells recovering from MreB depletion exhibit a strong budding and branching cell body phenotype and possess ectopic poles, as evidenced by the presence of multiple, misplaced, and sometimes highly branched stalks at the ends of these buds and branches. This phenotype is also seen to a lesser extent in cells recovering from RodA depletion and amdinocillin treatment. We conclude that MreB, RodA, and the target(s) of amdinocillin all contribute to the maintenance of cellular polarity in C. crescentus.

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.

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