› 5yqi

X-ray diffraction
1.6Å resolution

Crystal structure of the first StARkin domain of Lam2

Released:
DOI: 10.2210/pdb5yqi/pdb
PDB entry 5yqi coloured by chain, front view.
PDB entry 5yqi coloured by chain, side view.
PDB entry 5yqi coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural basis of sterol recognition and nonvesicular transport by lipid transfer proteins anchored at membrane contact sites.
Tong J, Manik MK, Im YJ
Proc Natl Acad Sci U S A 115 E856-E865 (2018)
PMID: 29339490

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-170374 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Membrane-anchored lipid-binding protein YSP2 Chain: A
Molecule details ›
Chain: A
Length: 171 amino acids
Theoretical weight: 19.24 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q06681 (Residues: 851-1016; Coverage: 12%)
Gene names: LAM2, LTC4, YDR326C, YSP2
Sequence domains: VAD1 Analog of StAR-related lipid transfer domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: P212121
Unit cell:
a: 33.433Å b: 59.505Å c: 84.29Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.246
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

15 review citations

Here, there, and everywhere: The importance of ER membrane contact sites.
Wu et al. (2018)
14 more

2 mentions without citation

The History and Science of the Major Birch Pollen Allergen Bet v 1.
Breiteneder et al. (2023)
1 more