› 4fmm

X-ray diffraction
2.34Å resolution

Dimeric Sec14 family homolog 3 from Saccharomyces cerevisiae presents some novel features of structure that lead to a surprising "dimer-monomer" state change induced by substrate binding

Released:
DOI: 10.2210/pdb4fmm/pdb
PDB entry 4fmm coloured by chain, front view.
PDB entry 4fmm coloured by chain, side view.
PDB entry 4fmm coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Dimeric Sfh3 has structural changes in its binding pocket that are associated with a dimer-monomer state transformation induced by substrate binding.
Yuan Y, Zhao W, Wang X, Gao Y, Niu L, Teng M
Acta Crystallogr D Biol Crystallogr 69 313-23 (2013)
PMID: 23519406

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156895 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphatidylinositol transfer protein PDR16 Chains: A, B
Molecule details ›
Chains: A, B
Length: 360 amino acids
Theoretical weight: 41.99 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P53860 (Residues: 1-351; Coverage: 100%)
Gene names: N1158, PDR16, SFH3, YNL231C
Sequence domains:
Structure domains: CRAL-TRIO lipid binding domain

Ligands and Environments

2 bound ligands:
Ligand GOL 9 x GOL
Ligand MG 3 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2221
Unit cell:
a: 76.177Å b: 76.914Å c: 294.956Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.214 0.264
Expression system: Escherichia coli BL21

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Citations

4 citation in other articles

The yeast Saccharomyces cerevisiae Pdr16p restricts changes in ergosterol biosynthesis caused by the presence of azole antifungals.
Šimová et al. (2013)
3 more

3 mentions without citation

PITPs as targets for selectively interfering with phosphoinositide signaling in cells.
Nile et al. (2014)
2 more