TY - JOUR
T1 - Regulation of the transcriptional activator NtrC1
T2 - Structural studies of the regulatory and AAA+ ATPase domains
AU - Lee, Seok Yong
AU - De La Torre, Armando
AU - Yan, Dalai
AU - Kustu, Sydney
AU - Nixon, B. Tracy
AU - Wemmer, David E.
PY - 2003/10/15
Y1 - 2003/10/15
N2 - Transcription by σ54 RNA polymerase depends on activators that contain ATPase domains of the AAA+ class. These activators, which are often response regulators of two-component signal transduction systems, remodel the polymerase so that it can form open complexes at promoters. Here, we report the first crystal structures of the ATPase domain of an activator, the NtrC1 protein from the extreme thermophile Aquifex aeolicus. This domain alone, which is active, crystallized as a ring-shaped heptamer. The protein carrying both the ATPase and adjacent receiver domains, which is inactive, crystallized as a dimer. In the inactive dimer, one residue needed for catalysis is far from the active site, and extensive contacts among the domains prevent oligomerization of the ATPase domain. Oligomerization, which completes the active site, depends on surfaces that are buried in the dimer, and hence, on a rearrangement of the receiver domains upon phosphorylation. A motif in the ATPase domain known to be critical for coupling energy to remodeling of polymerase forms a novel loop that projects from the middle of an α helix. The extended, structured loops from the subunits of the heptamer localize to a pore in the center of the ring and form a surface that could contact σ54.
AB - Transcription by σ54 RNA polymerase depends on activators that contain ATPase domains of the AAA+ class. These activators, which are often response regulators of two-component signal transduction systems, remodel the polymerase so that it can form open complexes at promoters. Here, we report the first crystal structures of the ATPase domain of an activator, the NtrC1 protein from the extreme thermophile Aquifex aeolicus. This domain alone, which is active, crystallized as a ring-shaped heptamer. The protein carrying both the ATPase and adjacent receiver domains, which is inactive, crystallized as a dimer. In the inactive dimer, one residue needed for catalysis is far from the active site, and extensive contacts among the domains prevent oligomerization of the ATPase domain. Oligomerization, which completes the active site, depends on surfaces that are buried in the dimer, and hence, on a rearrangement of the receiver domains upon phosphorylation. A motif in the ATPase domain known to be critical for coupling energy to remodeling of polymerase forms a novel loop that projects from the middle of an α helix. The extended, structured loops from the subunits of the heptamer localize to a pore in the center of the ring and form a surface that could contact σ54.
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U2 - 10.1101/gad.1125603
DO - 10.1101/gad.1125603
M3 - Article
C2 - 14561776
AN - SCOPUS:0142091549
SN - 0890-9369
VL - 17
SP - 2552
EP - 2563
JO - Genes and Development
JF - Genes and Development
IS - 20
ER -