› 2xju

X-ray diffraction
1.7Å resolution

X-ray structure of the N-terminal domain of the flocculin Flo5 from Saccharomyces cerevisiae with mutation S227A in complex with calcium and a1,2-mannobiose

Released:
DOI: 10.2210/pdb2xju/pdb
PDB entry 2xju coloured by chain, front view.
PDB entry 2xju coloured by chain, side view.
PDB entry 2xju coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Structural basis of flocculin-mediated social behavior in yeast.
Veelders M, Brückner S, Ott D, Unverzagt C, Mösch HU, Essen LO
Proc Natl Acad Sci U S A 107 22511-6 (2010)
PMID: 21149680

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153764 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Flocculation protein FLO5 Chain: A
Molecule details ›
Chain: A
Length: 258 amino acids
Theoretical weight: 27.72 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P38894 (Residues: 23-271; Coverage: 24%)
Gene names: FLO5, YHR211W
Sequence domains: PA14 domain
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: MAN
Carbohydrate polymer
4 bound ligands:
Ligand CA 2 x CA
Ligand NA 2 x NA
Ligand CL 1 x CL
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P212121
Unit cell:
a: 46.47Å b: 62.57Å c: 105.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.164 0.164 0.197
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Architecture and biosynthesis of the Saccharomyces cerevisiae cell wall.
Orlean P. (2012)
13 more

5 mentions without citation

Man-Specific Lectins from Plants, Fungi, Algae and Cyanobacteria, as Potential Blockers for SARS-CoV, MERS-CoV and SARS-CoV-2 (COVID-19) Coronaviruses: Biomedical Perspectives.
Barre et al. (2021)
4 more