2M1B

Solution structure of the CHXR DNA-binding domain

2M1B の概要

• エントリーDOI: 10.2210/pdb2m1b/pdb
• NMR情報: BMRB: 17014
• 分子名称: Transcriptional regulatory protein, C terminal family protein (1 entity in total)
• 機能のキーワード: ompr, transcription regulator
• 由来する生物種: Chlamydia trachomatis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13787.91

構造登録者

Hickey, J.M.,Anbanandam, A.M.,Hefty, S.P. (登録日: 2012-11-21, 公開日: 2014-03-26, 最終更新日: 2024-05-01)

主引用文献

Barta, M.L.,Hickey, J.M.,Anbanandam, A.,Dyer, K.,Hammel, M.,Hefty, P.S.
Atypical response regulator ChxR from Chlamydia trachomatis is structurally poised for DNA binding.
Plos One, 9:e91760-e91760, 2014

PubMed Abstract: ChxR is an atypical two-component signal transduction response regulator (RR) of the OmpR/PhoB subfamily encoded by the obligate intracellular bacterial pathogen Chlamydia trachomatis. Despite structural homology within both receiver and effector domains to prototypical subfamily members, ChxR does not require phosphorylation for dimer formation, DNA binding or transcriptional activation. Thus, we hypothesized that ChxR is in a conformation optimal for DNA binding with limited interdomain interactions. To address this hypothesis, the NMR solution structure of the ChxR effector domain was determined and used in combination with the previously reported ChxR receiver domain structure to generate a full-length dimer model based upon SAXS analysis. Small-angle scattering of ChxR supported a dimer with minimal interdomain interactions and effector domains in a conformation that appears to require only subtle reorientation for optimal major/minor groove DNA interactions. SAXS modeling also supported that the effector domains were in a head-to-tail conformation, consistent with ChxR recognizing tandem DNA repeats. The effector domain structure was leveraged to identify key residues that were critical for maintaining protein - nucleic acid interactions. In combination with prior analysis of the essential location of specific nucleotides for ChxR recognition of DNA, a model of the full-length ChxR dimer bound to its cognate cis-acting element was generated.

PubMed: 24646934
DOI: 10.1371/journal.pone.0091760

実験手法

SOLUTION NMR