› 5jqm

X-ray diffraction
1.5Å resolution

Crystal Structure of Phosphatidic acid Transporter Ups1/Mdm35 Void of Bound Phospholipid from Saccharomyces Cerevisiae at 1.5 Angstroms Resolution

Released:
DOI: 10.2210/pdb5jqm/pdb
PDB entry 5jqm coloured by chain, front view.
PDB entry 5jqm coloured by chain, side view.
PDB entry 5jqm coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Molecular mechanism of mitochondrial phosphatidate transfer by Ups1
Lu J, Chan C, Yu L, Fan J, Sun F, Zhai Y
Commun Biol (2020)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129906 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitochondrial distribution and morphology protein 35; Protein UPS1, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 283 amino acids
Theoretical weight: 32.35 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: Q05776 (Residues: 1-175; Coverage: 100%)
  • Canonical: O60200 (Residues: 1-86; Coverage: 100%)
Gene names: MDM35, UPS1, YKL053C-A, YLR193C
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2
Unit cell:
a: 118.563Å b: 68.29Å c: 105.137Å
α: 90° β: 102.1° γ: 90°
R-values:
R R work R free
0.166 0.164 0.202
Expression system: Escherichia coli

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Citations

2 review citations

Mechanisms of Non-Vesicular Exchange of Lipids at Membrane Contact Sites: Of Shuttles, Tunnels and, Funnels.
Egea PF. (2021)
1 more

1 mention without citation

Molecular mechanism of mitochondrial phosphatidate transfer by Ups1.
Lu et al. (2020)