› 2rkk

X-ray diffraction
2.9Å resolution

Crystal Structure of S.cerevisiae Vta1 N-terminal domain

Released:
DOI: 10.2210/pdb2rkk/pdb
PDB entry 2rkk coloured by chain, front view.
PDB entry 2rkk coloured by chain, side view.
PDB entry 2rkk coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural basis of Vta1 function in the multivesicular body sorting pathway.
Xiao J, Xia H, Zhou J, Azmi IF, Davies BA, Katzmann DJ, Xu Z
Dev Cell 14 37-49 (2008)
PMID: 18194651

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170317 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vacuolar protein sorting-associated protein VTA1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 168 amino acids
Theoretical weight: 19.15 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q06263 (Residues: 1-167; Coverage: 51%)
Gene names: VTA1, YLR181C
Sequence domains: Vta1 like
Structure domains: Vacuolar protein sorting-associated protein vta1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: I4
Unit cell:
a: 126.169Å b: 126.169Å c: 70.252Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.215 0.26
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

16 review citations

Membrane budding and scission by the ESCRT machinery: it's all in the neck.
Hurley et al. (2010)
15 more

6 mentions without citation

Structural basis of Vta1 function in the multivesicular body sorting pathway.
Xiao et al. (2008)
5 more