› 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 entry 3g9h coloured by chain, front view.
PDB entry 3g9h coloured by chain, side view.
PDB entry 3g9h coloured by chain, top view.
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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150523 (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 mechanism and physiological functions of clathrin-mediated endocytosis.
McMahon et al. (2011)
26 more

5 mentions without citation

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