8CR3

Crystal structure of recombinant LasB from Pseudomonas aeruginosa PAO1

Summary for 8CR3

• Entry DOI: 10.2210/pdb8cr3/pdb
• Descriptor: Pro-elastase, ZINC ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: lasb, pseudomonas aeruginosa, recombinant, hydrolase
• Biological source: Pseudomonas aeruginosa PAO1
• Total number of polymer chains: 1
• Total formula weight: 55778.40

Authors

Kolling, D.,Koehnke, J. (deposition date: 2023-03-07, release date: 2023-07-05, Last modification date: 2024-10-09)

Primary citation

Kolling, D.,Haupenthal, J.,Hirsch, A.K.H.,Koehnke, J.
Facile Production of the Pseudomonas aeruginosa Virulence Factor LasB in Escherichia coli for Structure-Based Drug Design.
Chembiochem, 24:e202300185-e202300185, 2023

PubMed Abstract: The human pathogen Pseudomonas aeruginosa has a number of virulence factors at its disposal that play crucial roles in the progression of infection. LasB is one of the major virulence factors and exerts its effects through elastolytic and proteolytic activities aimed at dissolving connective tissue and inactivating host defense proteins. LasB is of great interest for the development of novel pathoblockers to temper the virulence, but access has thus far largely been limited to protein isolated from Pseudomonas cultures. Here, we describe a new protocol for high-level production of native LasB in Escherichia coli. We demonstrate that this facile approach is suitable for the production of mutant, thus far inaccessible LasB variants, and characterize the proteins biochemically and structurally. We expect that easy access to LasB will accelerate the development of inhibitors for this important virulence factor.

PubMed: 37195753
DOI: 10.1002/cbic.202300185

Experimental method

X-RAY DIFFRACTION (1.12 Å)