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TitleHigh-resolution crystal structures of two prototypical beta- and gamma-herpesviral nuclear egress complexes unravel the determinants of subfamily specificity.
Journal, issue, pagesJ. Biol. Chem., Vol. 295, Page 3189-3201, Year 2020
Publish dateOct 11, 2019 (structure data deposition date)
AuthorsMuller, Y.A. / Hage, S. / Alkhashrom, S. / Hollriegl, T. / Weigert, S. / Dolles, S. / Hof, K. / Walzer, S.A. / Egerer-Sieber, C. / Conrad, M. ...Muller, Y.A. / Hage, S. / Alkhashrom, S. / Hollriegl, T. / Weigert, S. / Dolles, S. / Hof, K. / Walzer, S.A. / Egerer-Sieber, C. / Conrad, M. / Holst, S. / Losing, J. / Sonntag, E. / Sticht, H. / Eichler, J. / Marschall, M.
External linksJ. Biol. Chem. / PubMed:31980459
MethodsX-ray diffraction
Resolution1.48 - 1.55862788727 Å
Structure data

PDB-6t3x:
Crystal structure of the truncated human cytomegalovirus pUL50-pUL53 complex
Method: X-RAY DIFFRACTION / Resolution: 1.48 Å

PDB-6t3z:
Crystal structure of the truncated EBV BFRF1-BFLF2 nuclear egress complex
Method: X-RAY DIFFRACTION / Resolution: 1.55862788727 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-MLI:
MALONATE ION

Source
  • human cytomegalovirus (strain ad169)
  • epstein-barr virus (strain gd1) (Epstein-Barr virus)
KeywordsVIRAL PROTEIN / nuclear egress / fusion protein / Nuclear egress complex / Epstein-Barr virus / gamma-herpesviral core NEC

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