The crystal structure of CbpD clarifies substrate-specificity motifs in chitin-active lytic polysaccharide monooxygenases

Autor: Christopher M. Dade, Badreddine Douzi, Christian Cambillau, Genevieve Ball, Romé Voulhoux, Katrina T. Forest

Publikováno v: Acta crystallographica Section D : Structural biology [1993-...]
Acta crystallographica Section D : Structural biology [1993-..], 2022, 78 (8), pp.1064-1078. ⟨10.1107/S2059798322007033⟩

Pseudomonas aeruginosa secretes diverse proteins via its type 2 secretion system, including a 39 kDa chitin-binding protein, CbpD. CbpD has recently been shown to be a lytic polysaccharide monooxygenase active on chitin and to contribute substantiall

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cb869f94899dc1aff80c91f327ef4407
https://hal.science/hal-03739502/file/jc5051.pdf

A novel extracellular phospholipase C of Pseudomonas aeruginosa is required for phospholipid chemotaxis

Autor: Adam P, Barker, Adriana I, Vasil, Alain, Filloux, Genevieve, Ball, Paula J, Wilderman, Michael L, Vasil

Publikováno v: Molecular microbiology. 53(4)

Pseudomonas aeruginosa and other bacterial pathogens express one or more homologous extracellular phospholipases C (PLC) that are secreted through the inner membrane via the twin arginine translocase (TAT) pathway. Analysis of TAT mutants of P. aerug

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6ccc5fc2b4098f363cdfd83a450890aa
https://pubmed.ncbi.nlm.nih.gov/15306013