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Structure paper

TitleStructural basis of flagellar motility regulation by the MogR repressor and the GmaR antirepressor in Listeria monocytogenes.
Journal, issue, pagesNucleic Acids Res., Vol. 50, Page 11315-11330, Year 2022
Publish dateMar 16, 2022 (structure data deposition date)
AuthorsCho, S.Y. / Na, H.W. / Oh, H.B. / Kwak, Y.M. / Song, W.S. / Park, S.C. / Jeon, W.J. / Cho, H. / Oh, B.C. / Park, J. ...Cho, S.Y. / Na, H.W. / Oh, H.B. / Kwak, Y.M. / Song, W.S. / Park, S.C. / Jeon, W.J. / Cho, H. / Oh, B.C. / Park, J. / Kang, S.G. / Lee, G.S. / Yoon, S.I.
External linksNucleic Acids Res. / PubMed:36283692
MethodsX-ray diffraction
Resolution2.25 - 3.11 Å
Structure data

PDB-7x9r:
Crystal structure of the antirepressor GmaR
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

PDB-7x9s:
Crystal structure of a complex between the antirepressor GmaR and the transcriptional repressor MogR
Method: X-RAY DIFFRACTION / Resolution: 3.11 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • listeria monocytogenes (bacteria)
KeywordsPROTEIN BINDING / Antirepressor / PROTEIN BINDING/TRANSCRIPTION / repressor / TRANSFERASE / PROTEIN BINDING-TRANSCRIPTION complex

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