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TitleNucleotide-induced asymmetry within ATPase activator ring drives σ54-RNAP interaction and ATP hydrolysis.
Journal, issue, pagesGenes Dev, Vol. 27, Issue 22, Page 2500-2511, Year 2013
Publish dateNov 15, 2013
AuthorsTatyana A Sysoeva / Saikat Chowdhury / Liang Guo / B Tracy Nixon /
PubMed AbstractIt is largely unknown how the typical homomeric ring geometry of ATPases associated with various cellular activities enables them to perform mechanical work. Small-angle solution X-ray scattering, ...It is largely unknown how the typical homomeric ring geometry of ATPases associated with various cellular activities enables them to perform mechanical work. Small-angle solution X-ray scattering, crystallography, and electron microscopy (EM) reconstructions revealed that partial ATP occupancy caused the heptameric closed ring of the bacterial enhancer-binding protein (bEBP) NtrC1 to rearrange into a hexameric split ring of striking asymmetry. The highly conserved and functionally crucial GAFTGA loops responsible for interacting with σ54-RNA polymerase formed a spiral staircase. We propose that splitting of the ensemble directs ATP hydrolysis within the oligomer, and the ring's asymmetry guides interaction between ATPase and the complex of σ54 and promoter DNA. Similarity between the structure of the transcriptional activator NtrC1 and those of distantly related helicases Rho and E1 reveals a general mechanism in homomeric ATPases whereby complex allostery within the ring geometry forms asymmetric functional states that allow these biological motors to exert directional forces on their target macromolecules.
External linksGenes Dev / PubMed:24240239 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.21 - 24.0 Å
Structure data

EMDB-5698:
Structure of NtrC1 ATPase in complex with Sigma-54 and promoter DNA
Method: EM (single particle) / Resolution: 24.0 Å

PDB-4ly6:
Nucleotide-induced asymmetry within ATPase activator ring drives s54-RNAP interaction and ATP hydrolysis
Method: X-RAY DIFFRACTION / Resolution: 3.6 Å

PDB-4lzz:
Nucleotide-induced asymmetry within atpase activator ring drives s54-RNAP interaction and ATP hydrolysis
Method: X-RAY DIFFRACTION / Resolution: 3.21 Å

Chemicals

ChemComp-08T:
[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-tris(fluoranyl)beryllium

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • aquifex aeolicus (bacteria)
  • Klebsiella pneumoniae (bacteria)
  • Sinorhizobium meliloti (bacteria)
KeywordsTRANSCRIPTION REGULATOR / AAA+ ATPase / bacterial enhancer binding protein / s54-dependent transcription activator / molecular machine / sigma54 / s54-RNAP

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