8cr4

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== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/ELAS_PSEAB ELAS_PSEAB] Cleaves host elastase, collagen, IgI and several complement components as well as endogenous pro-aminopeptidase, pro-chitin-binding protein (cbpD). Cleaves its own pro-peptide. Involved in the pathogenesis of P.aeruginosa infections.[UniProtKB:P14756]
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[https://www.uniprot.org/uniprot/ELAS_PSEAE ELAS_PSEAE] Cleaves elastin, collagen, IgG, and several complement components. Involved in the pathogenesis of P.aeruginosa infections.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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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 patho-blockers 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 E. 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 is going to accelerate the development of inhibitors for this important virulence factor.
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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.
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Facile Production of the Pseudomonas aeruginosa Virulence Factor LasB in E. coli for Structure-Based Drug Design.,Kolling D, Haupenthal J, Hirsch AKH, Kohnke J Chembiochem. 2023 May 17:e202300185. doi: 10.1002/cbic.202300185. PMID:37195753<ref>PMID:37195753</ref>
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Facile Production of the Pseudomonas aeruginosa Virulence Factor LasB in Escherichia coli for Structure-Based Drug Design.,Kolling D, Haupenthal J, Hirsch AKH, Koehnke J Chembiochem. 2023 Sep 1;24(17):e202300185. doi: 10.1002/cbic.202300185. Epub 2023 , Jul 31. PMID:37195753<ref>PMID:37195753</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

Current revision

Crystal structure of recombinant LasBArtif from Pseudomonas aeruginosa AZPAE14816

PDB ID 8cr4

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