CyberinfraV1, Main, Exploration, bibRecord, 000308

Nucleotide-induced asymmetry within ATPase activator ring drives σ54–RNAP interaction and ATP hydrolysis

Identifieur interne : 000308 ( Main/Exploration ); précédent : 000307; suivant : 000309

Nucleotide-induced asymmetry within ATPase activator ring drives σ54–RNAP interaction and ATP hydrolysis

Auteurs : Tatyana A. Sysoeva [États-Unis] ; Saikat Chowdhury [États-Unis] ; Liang Guo [États-Unis] ; B. Tracy Nixon [États-Unis]

Source :

Genes & Development [ 0890-9369 ] ; 2013.

RBID : PMC:3841738

Abstract

AAA⁺ ATPase molecular machines perform mechanical work in all organisms. A key question is how rings of identical subunits interact with asymmetric target macromolecules. This study by Nixon and colleagues elucidates the structure of AAA⁺ ATPase bacterial transcriptional activator NtrC1, providing mechanistic insight into transcription initiation. Partial ATP occupancy causes the heptameric closed ring of NtrC1 to rearrange into a hexameric split ring of striking asymmetry. Furthermore, the similarity between the structure of NtrC1 and those of distantly related helicases reveals a general mechanism for homomeric ATPase function.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3841738

DOI: 10.1101/gad.229385.113
PubMed: 24240239
PubMed Central: 3841738

Affiliations:

Le document en format XML

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 ATPase molecular machines perform mechanical work in all organisms. A key question is how rings of identical subunits interact with asymmetric target macromolecules. This study by Nixon and colleagues elucidates the structure of AAA<sup>+</sup>
 ATPase bacterial transcriptional activator NtrC1, providing mechanistic insight into transcription initiation. Partial ATP occupancy causes the heptameric closed ring of NtrC1 to rearrange into a hexameric split ring of striking asymmetry. Furthermore, the similarity between the structure of NtrC1 and those of distantly related helicases reveals a general mechanism for homomeric ATPase function.</p>
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Nucleotide-induced asymmetry within ATPase activator ring drives σ54–RNAP interaction and ATP hydrolysis

Nucleotide-induced asymmetry within ATPase activator ring drives σ54–RNAP interaction and ATP hydrolysis

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Abstract

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