2Y7N: Structure Of N-Terminal Domain Of Candida Albicans Als9-2 - Apo Form

Citation:
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.
PDB ID: 2Y7NDownload
MMDB ID: 93997
PDB Deposition Date: 2011/1/31
Updated in MMDB: 2011/10
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 2Y7N: monomeric; determined by author and by software (PISA)
Molecular Components in 2Y7N
Label Count Molecule
Protein (1 molecule)
1
Agglutinin-like Als9 Protein
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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