2Y7M

Structure of N-terminal domain of Candida albicans als9-2 (Pt derivative)

Summary for 2Y7M

• Entry DOI: 10.2210/pdb2y7m/pdb
• Related: 2Y7L 2Y7N 2Y7O
• Descriptor: AGGLUTININ-LIKE ALS9 PROTEIN (2 entities in total)
• Functional Keywords: cell adhesion, peptide binding protein
• Biological source: CANDIDA ALBICANS
• Total number of polymer chains: 1
• Total formula weight: 33573.99

Authors

Salgado, P.S.,Cota, E. (deposition date: 2011-01-31, release date: 2011-10-05, Last modification date: 2024-10-09)

Primary citation

Salgado, P.S.,Yan, R.,Taylor, J.D.,Burchell, L.,Jones, R.,Hoyer, L.L.,Matthews, S.J.,Simpson, P.J.,Cota, E.
Structural basis for the broad specificity to host-cell ligands by the pathogenic fungus Candida albicans.
Proc. Natl. Acad. Sci. U.S.A., 108:15775-15779, 2011

PubMed Abstract: Candida albicans is the most prevalent fungal pathogen in humans and a major source of life-threatening nosocomial infections. The Als (agglutinin-like sequence) glycoproteins are an important virulence factor for this fungus and have been associated with binding of host-cell surface proteins and small peptides of random sequence, the formation of biofilms and amyloid fibers. High-resolution structures of N-terminal Als adhesins (NT-Als; up to 314 amino acids) show that ligand recognition relies on a motif capable of binding flexible C termini of peptides in extended conformation. Central to this mechanism is an invariant lysine that recognizes the C-terminal carboxylate of ligands at the end of a deep-binding cavity. In addition to several protein-peptide interactions, a network of water molecules runs parallel to one side of the ligand and contributes to the recognition of diverse peptide sequences. These data establish NT-Als adhesins as a separate family of peptide-binding proteins and an unexpected adhesion system for primary, widespread protein-protein interactions at the Candida/host-cell interface.

PubMed: 21896717
DOI: 10.1073/pnas.1103496108

Experimental method

X-RAY DIFFRACTION (1.98 Å)