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Structure paper

TitleA Flexible and Original Architecture of Two Unrelated Zinc Fingers Underlies the Role of the Multitask P1 in RYMV Spread.
Journal, issue, pagesJ. Mol. Biol., Vol. 434, Page 167715-167715, Year 2022
Publish dateJan 15, 2020 (structure data deposition date)
AuthorsPoignavent, V. / Hoh, F. / Terral, G. / Yang, Y. / Gillet, F.X. / Kim, J.H. / Allemand, F. / Lacombe, E. / Brugidou, C. / Cianferani, S. ...Poignavent, V. / Hoh, F. / Terral, G. / Yang, Y. / Gillet, F.X. / Kim, J.H. / Allemand, F. / Lacombe, E. / Brugidou, C. / Cianferani, S. / Demene, H. / Vignols, F.
External linksJ. Mol. Biol. / PubMed:35798161
MethodsX-ray diffraction / NMR (solution)
Resolution1.98 - 2.1 Å
Structure data

PDB-6ty0:
NT PART CRYSTAL STRUCTURE OF THE RYMV-ENCODED VIRAL RNA SILENCING SUPPRESSOR P1
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-6ty2:
CT PART CRYSTAL STRUCTURE OF THE RYMV-ENCODED VIRAL RNA SILENCING SUPPRESSOR P1
Method: X-RAY DIFFRACTION / Resolution: 1.98 Å

PDB-6xv2:
Full structure of RYMV P1 protein, derived from crystallographic and NMR data.
Method: SOLUTION NMR

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • rice yellow mottle virus
KeywordsRNA BINDING PROTEIN / ZINC FINGERS / RNA SILENCING SUPPRESSOR / VIRAL PROTEIN / putative RNA binding protein; silencing suppressor

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