4LY6
Nucleotide-induced asymmetry within ATPase activator ring drives s54-RNAP interaction and ATP hydrolysis
Summary for 4LY6
| Entry DOI | 10.2210/pdb4ly6/pdb |
| Related | 4LZZ |
| Descriptor | Transcriptional regulator (NtrC family), [[[(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, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | aaa+ atpase, bacterial enhancer binding protein, s54-dependent transcription activator, molecular machine, sigma54, s54-rnap, transcription regulator |
| Biological source | Aquifex aeolicus |
| Total number of polymer chains | 24 |
| Total formula weight | 748742.87 |
| Authors | Sysoeva, T.A.,Chowdhury, S.,Guo, L.,Nixon, B.T. (deposition date: 2013-07-30, release date: 2013-12-04, Last modification date: 2024-02-28) |
| Primary citation | Sysoeva, T.A.,Chowdhury, S.,Guo, L.,Nixon, B.T. Nucleotide-induced asymmetry within ATPase activator ring drives sigma 54-RNAP interaction and ATP hydrolysis. Genes Dev., 27:2500-2511, 2013 Cited by PubMed Abstract: 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. PubMed: 24240239DOI: 10.1101/gad.229385.113 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.6 Å) |
Structure validation
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