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Cell-Wall Remodeling by the Zinc-Protease AmpDh3 from Pseudomonas aeruginosa
Cell-Wall Remodeling by the Zinc-Protease AmpDh3 from Pseudomonas aeruginosa
- Source :
- Digital.CSIC. Repositorio Institucional del CSIC, instname
- Publication Year :
- 2013
- Publisher :
- American Chemical Society (ACS), 2013.
-
Abstract
- Bacterial cell wall is a polymer of considerable complexity that is in constant equilibrium between synthesis and recycling. AmpDh3 is a periplasmic zinc protease of Pseudomonas aeruginosa, which is intimately involved in cell-wall remodeling. We document the hydrolytic reactions that this enzyme performs on the cell wall. The process removes the peptide stems from the peptidoglycan, the major constituent of the cell wall. We document that the majority of the reactions of this enzyme takes place on the polymeric insoluble portion of the cell wall, as opposed to the fraction that is released from it. We show that AmpDh3 is tetrameric both in crystals and in solution. Based on the X-ray structures of the enzyme in complex with two synthetic cell-wall-based ligands, we present for the first time a model for a multivalent anchoring of AmpDh3 onto the cell wall, which lends itself to its processive remodeling. © 2013 American Chemical Society.
- Subjects :
- Models, Molecular
medicine.medical_treatment
Molecular Conformation
Crystallography, X-Ray
Biochemistry
Article
Catalysis
Bacterial cell structure
Cell wall
chemistry.chemical_compound
Colloid and Surface Chemistry
Cell Wall
Hydrolase
medicine
chemistry.chemical_classification
Metalloproteinase
Protease
General Chemistry
Periplasmic space
Zinc
Enzyme
chemistry
Pseudomonas aeruginosa
Metalloproteases
Peptidoglycan
Subjects
Details
- ISSN :
- 15205126 and 00027863
- Volume :
- 135
- Database :
- OpenAIRE
- Journal :
- Journal of the American Chemical Society
- Accession number :
- edsair.doi.dedup.....41f9eeeba1b6082b1dfd19033f476d14
- Full Text :
- https://doi.org/10.1021/ja407445x