› 2w6d

Electron Microscopy
9Å resolution

BACTERIAL DYNAMIN-LIKE PROTEIN LIPID TUBE BOUND

Released:
DOI: 10.2210/pdb2w6d/pdb
PDB entry 2w6d coloured by chain, front view.
PDB entry 2w6d coloured by chain, side view.
PDB entry 2w6d coloured by chain, top view.
Source organism: Nostoc punctiforme PCC 73102
Primary publication:
Structure of a bacterial dynamin-like protein lipid tube provides a mechanism for assembly and membrane curving.
Low HH, Sachse C, Amos LA, Löwe J
Cell 139 1342-52 (2009)
PMID: 20064379
Related structures: EMD-1589

Function and Biology Details

Reaction catalysed: 
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109617 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bacterial dynamin-like protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 695 amino acids
Theoretical weight: 78.72 KDa
Source organism: Nostoc punctiforme PCC 73102
Expression system: Escherichia coli
UniProt:
  • Canonical: B2IZD3 (Residues: 1-693; Coverage: 100%)
Gene name: Npun_R6513
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand CPL 44 x CPL
Ligand GDP 2 x GDP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 9Å
Relevant EMDB volumes: EMD-1589
Expression system: Escherichia coli

Quick links

Citations

37 review citations

Dynamin, a membrane-remodelling GTPase.
Ferguson et al. (2012)
36 more

17 mentions without citation

Invited review: Mechanisms of GTP hydrolysis and conformational transitions in the dynamin superfamily.
Daumke et al. (2016)
16 more