› 9eon

Electron Microscopy
6.4Å resolution

270A Vipp1 dL10Ala helical tubes in the presence of EPL

Released:
DOI: 10.2210/pdb9eon/pdb
PDB entry 9eon coloured by chain, front view.
PDB entry 9eon coloured by chain, side view.
PDB entry 9eon coloured by chain, top view.
Source organism: Synechocystis sp. PCC 6803
Primary publication:
Structural basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies.
Junglas B, Kartte D, Kutzner M, Hellmann N, Ritter I, Schneider D, Sachse C
Nat Struct Mol Biol (2024)
PMID: 39379528
Related structures: EMD-19864

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo 60-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-280642 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Membrane-associated protein Vipp1 Chain: A
Molecule details ›
Chain: A
Length: 277 amino acids
Theoretical weight: 29.86 KDa
Source organism: Synechocystis sp. PCC 6803
Expression system: Escherichia coli
UniProt:
  • Canonical: Q55707 (Residues: 1-267; Coverage: 100%)
Gene names: sll0617, vipp1
Sequence domains: PspA/IM30 family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 6.4Å
Relevant EMDB volumes: EMD-19864
Expression system: Escherichia coli

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