› 4txp

X-ray diffraction
3.01Å resolution

Crystal structure of LIP5 N-terminal domain

Released:
DOI: 10.2210/pdb4txp/pdb
PDB entry 4txp coloured by chain, front view.
PDB entry 4txp coloured by chain, side view.
PDB entry 4txp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A novel mechanism of regulating the ATPase VPS4 by its cofactor LIP5 and the endosomal sorting complex required for transport (ESCRT)-III protein CHMP5.
Vild CJ, Li Y, Guo EZ, Liu Y, Xu Z
J Biol Chem 290 7291-303 (2015)
PMID: 25637630

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192460 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vacuolar protein sorting-associated protein VTA1 homolog Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 163 amino acids
Theoretical weight: 18.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NP79 (Residues: 1-162; Coverage: 53%)
Gene names: C6orf55, HSPC228, My012, VTA1
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: P6522
Unit cell:
a: 76.381Å b: 76.381Å c: 355.938Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.25 0.248 0.286
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Meiotic Clade AAA ATPases: Protein Polymer Disassembly Machines.
Monroe et al. (2016)
3 more

4 mentions without citation

Distinct mechanisms of recognizing endosomal sorting complex required for transport III (ESCRT-III) protein IST1 by different microtubule interacting and trafficking (MIT) domains.
Guo et al. (2015)
3 more