› 3g9h

X-ray diffraction
2.8Å resolution

Crystal structure of the C-terminal mu homology domain of Syp1

Released:
DOI: 10.2210/pdb3g9h/pdb
PDB 3g9h coloured by chain and viewed from the front.
PDB 3g9h coloured by chain and viewed from the side.
PDB 3g9h coloured by chain and viewed from the top.
Source organism: Saccharomyces cerevisiae
Primary publication:
Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation.
Reider A, Barker SL, Mishra SK, Im YJ, Maldonado-Báez L, Hurley JH, Traub LM, Wendland B
EMBO J. 28 3103-16 (2009)
PMID: 19713939

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Suppressor of yeast profilin deletion Chain: A
Molecule details ›
Chain: A
Length: 328 amino acids
Theoretical weight: 35.69 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P25623 (Residues: 566-870; Coverage: 35%)
Gene names: SYP1, YCR030C, YCR30C/YCR29C
Sequence domains: Muniscin C-terminal mu homology domain

Ligands and Environments

1 bound ligand:
Ligand 1PG 1 x 1PG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P6122
Unit cell:
a: 134.063Å b: 134.063Å c: 93.703Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.261 0.232 0.275
Expression system: Escherichia coli

Quick links

Citations

27 review citations

Molecular mechanisms of endomembrane trafficking in plants.
Aniento et al. (2022)
26 more

5 mentions without citation

Molecular structure, function, and dynamics of clathrin-mediated membrane traffic.
Kirchhausen et al. (2014)
4 more