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Baikalov I., Schröder I., Kaczor-Grzeskowiak M., Grzeskowiak K., Gunsalus R.P., and Dickerson R.E. Structure of the Escherichia coli response regulator NarL. Biochemistry 35 (1996) 11053-11061
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Dickerson, R.E.6
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Crystal structures of the response regulator DosR from Mycobacterium tuberculosis suggest a helix rearrangement mechanism for phosphorylation activation
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Structures of a full-length NarL subfamily transcription factor DosR reveal an unusual β4α4 fold for the receiver domain. Dimerization is mediated by two linker helices in each protomer that participate in a four-helix bundle domain interface. In inactive DosR, interdomain contacts include an interaction between helix α10 of the effector domain and Asp54 at the phosphorylation site of the receiver domain. Phosphorylation-mediated activation of DosR is proposed to involve disruption of this contact and rearrangement of helix α10.
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Wisedchaisri G., Wu M., Sherman D.R., and Hol W.G. Crystal structures of the response regulator DosR from Mycobacterium tuberculosis suggest a helix rearrangement mechanism for phosphorylation activation. J Mol Biol 378 (2008) 227-242. Structures of a full-length NarL subfamily transcription factor DosR reveal an unusual β4α4 fold for the receiver domain. Dimerization is mediated by two linker helices in each protomer that participate in a four-helix bundle domain interface. In inactive DosR, interdomain contacts include an interaction between helix α10 of the effector domain and Asp54 at the phosphorylation site of the receiver domain. Phosphorylation-mediated activation of DosR is proposed to involve disruption of this contact and rearrangement of helix α10.
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Wisedchaisri, G.1
Wu, M.2
Sherman, D.R.3
Hol, W.G.4
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Structural analysis of the domain interface in DrrB, a response regulator of the OmpR/PhoB subfamily
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Robinson V.L., Wu T., and Stock A.M. Structural analysis of the domain interface in DrrB, a response regulator of the OmpR/PhoB subfamily. J Bacteriol 185 (2003) 4186-4194
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Stock, A.M.3
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Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima
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Buckler D.R., Zhou Y., and Stock A.M. Evidence of intradomain and interdomain flexibility in an OmpR/PhoB homolog from Thermotoga maritima. Structure 10 (2002) 153-164
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Buckler, D.R.1
Zhou, Y.2
Stock, A.M.3
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The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis
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Nowak E., Panjikar S., Konarev P., Svergun D.I., and Tucker P.A. The structural basis of signal transduction for the response regulator PrrA from Mycobacterium tuberculosis. J Biol Chem 281 (2006) 9659-9666
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Nowak, E.1
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Tucker, P.A.5
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47
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Domain orientation in the inactive response regulator Mycobacterium tuberculosis MtrA provides a barrier to activation
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Friedland N., Mack T.R., Yu M., Hung L.-W., Terwilliger T.C., Waldo G.S., and Stock A.M. Domain orientation in the inactive response regulator Mycobacterium tuberculosis MtrA provides a barrier to activation. Biochemistry 46 (2007) 6733-6743
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Friedland, N.1
Mack, T.R.2
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Hung, L.-W.4
Terwilliger, T.C.5
Waldo, G.S.6
Stock, A.M.7
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Structural and mechanistic determinants of c-di-GMP signalling
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Schirmer T., and Jenal U. Structural and mechanistic determinants of c-di-GMP signalling. Nat Rev Microbiol 7 (2009) 724-735
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