› 4lzz

X-ray diffraction
3.21Å resolution

Nucleotide-induced asymmetry within atpase activator ring drives s54-RNAP interaction and ATP hydrolysis

Released:
DOI: 10.2210/pdb4lzz/pdb
PDB entry 4lzz coloured by chain, front view.
PDB entry 4lzz coloured by chain, side view.
PDB entry 4lzz coloured by chain, top view.
Source organism: Aquifex aeolicus
Primary publication:
Nucleotide-induced asymmetry within ATPase activator ring drives σ54-RNAP interaction and ATP hydrolysis.
Sysoeva TA, Chowdhury S, Guo L, Nixon BT
OpenAccess logo Genes Dev 27 2500-11 (2013)
PMID: 24240239

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130470 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcriptional regulator (NtrC family) Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Length: 268 amino acids
Theoretical weight: 30.73 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O67198 (Residues: 121-387; Coverage: 61%)
Gene names: aq_1117, ntrC1
Sequence domains: Sigma-54 interaction domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand 08T 22 x 08T
Ligand MG 23 x MG
Ligand ADP 2 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P1
Unit cell:
a: 119.97Å b: 130.83Å c: 208.23Å
α: 90.01° β: 90.01° γ: 89.85°
R-values:
R R work R free
0.268 0.267 0.322
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Mechanistic and Structural Insights into the Prion-Disaggregase Activity of Hsp104.
Sweeny et al. (2016)
8 more

2 mentions without citation

Nucleotide-induced asymmetry within ATPase activator ring drives σ54-RNAP interaction and ATP hydrolysis.
Sysoeva et al. (2013)
1 more