The crystal structure of CbpD clarifies substrate-specificity motifs in chitin-active lytic polysaccharide monooxygenases - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Acta crystallographica Section D : Structural biology [1993-...] Année : 2022

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

Résumé

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 substantially to virulence. To date, no structure of this virulence factor has been reported. Its first two domains are homologous to those found in the crystal structure of Vibrio cholerae GbpA, while the third domain is homologous to the NMR structure of the CBM73 domain of Cellvibrio japonicus Cj LPMO10A. Here, the 3.0 Å resolution crystal structure of CbpD solved by molecular replacement is reported, which required ab initio models of each CbpD domain generated by the artificial intelligence deep-learning structure-prediction algorithm RoseTTAFold . The structure of CbpD confirms some previously reported substrate-specificity motifs among LPMOAA10s, while challenging the predictive power of others. Additionally, the structure of CbpD shows that post-translational modifications occur on the chitin-binding surface. Moreover, the structure raises interesting possibilities about how type 2 secretion-system substrates may interact with the secretion machinery and demonstrates the utility of new artificial intelligence protein structure-prediction algorithms in making challenging structural targets tractable.
Fichier principal
Vignette du fichier
jc5051.pdf (2.11 Mo) Télécharger le fichier
Origine : Publication financée par une institution

Dates et versions

hal-03739502 , version 1 (27-07-2022)

Identifiants

Citer

Christopher Dade, Badreddine Douzi, Christian Cambillau, Genevieve Ball, Romé Voulhoux, et al.. The crystal structure of CbpD clarifies substrate-specificity motifs in chitin-active lytic polysaccharide monooxygenases. Acta crystallographica Section D : Structural biology [1993-..], 2022, 78 (8), pp.1064-1078. ⟨10.1107/S2059798322007033⟩. ⟨hal-03739502⟩
66 Consultations
24 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More