7O9Q

Crystal structure of the Awp1 (adhesin-like wall protein 1) A-domain from Candida glabrata

Summary for 7O9Q

• Entry DOI: 10.2210/pdb7o9q/pdb
• Descriptor: Awp1A, pentane-1,5-diol (3 entities in total)
• Functional Keywords: candida glabrata, adhesin, adhesion, awp, adhesin-like wall protein, beta-helix, haze-protective factor, cell adhesion
• Biological source: [Candida] glabrata
• Total number of polymer chains: 2
• Total formula weight: 71759.26

Authors

Reithofer, V.,de Groot, P.,Essen, L.-O. (deposition date: 2021-04-16, release date: 2021-12-15, Last modification date: 2024-05-01)

Primary citation

Reithofer, V.,Fernandez-Pereira, J.,Alvarado, M.,de Groot, P.,Essen, L.O.
A novel class of Candida glabrata cell wall proteins with beta-helix fold mediates adhesion in clinical isolates.
Plos Pathog., 17:e1009980-e1009980, 2021

PubMed Abstract: Candida glabrata is an opportunistic pathogenic yeast frequently causing infections in humans. Though it lacks typical virulence factors such as hyphal development, C. glabrata contains a remarkably large and diverse set of putative wall adhesins that is crucial for its success as pathogen. Here, we present an analysis of putative adhesins from the homology clusters V and VI. First, sequence similarity network analysis revealed relationships between cluster V and VI adhesins and S. cerevisiae haze protective factors (Hpf). Crystal structures of A-regions from cluster VI adhesins Awp1 and Awp3b reveal a parallel right-handed β-helix domain that is linked to a C-terminal β-sandwich. Structure solution of the A-region of Awp3b via single wavelength anomalous diffraction phasing revealed the largest known lanthanide cluster with 21 Gd3+ ions. Awp1-A and Awp3b-A show structural similarity to pectate lyases but binding to neither carbohydrates nor Ca2+ was observed. Phenotypic analysis of awp1Δ, awp3Δ, and awp1,3Δ double mutants did also not confirm their role as adhesins. In contrast, deletion mutants of the cluster V adhesin Awp2 in the hyperadhesive clinical isolate PEU382 demonstrated its importance for adhesion to polystyrene or glass, biofilm formation, cell aggregation and other cell surface-related phenotypes. Together with cluster III and VII adhesins our study shows that C. glabrata CBS138 can rely on a set of 42 Awp1-related adhesins with β-helix/α-crystallin domain architecture for modifying the surface characteristics of its cell wall.

PubMed: 34962966
DOI: 10.1371/journal.ppat.1009980

Experimental method

X-RAY DIFFRACTION (1.85 Å)