Structure of the Reston ebolavirus VP30 C-terminal domain

Clifton, M.C.; Kirchdoerfer, R.N.; Atkins, K.; Abendroth, J.; Raymond, A.; Grice, R.; Barnes, S.; Moen, S.; Lorimer, D.; Edwards, T.E.; Myler, P.J.; Saphire, E.O.

doi:10.1107/S2053230X14003811

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 1
Overall Reston ebolavirus VP30 C-terminal domain structure. (a) Attempted cleavage of Smt-VP30 CTD with Ulp-1 protease. Lane 1, protein marker (labeled in kDa); lane 2, undigested protein; lane 3, Ulp-1 digestion. (b) The VP30 monomers forming the dimer are shown in orange and yellow. The ordered Smt domain is attached to the yellow VP30. The image is shown in wall-eyed stereo. (c) Sequence alignment of VP30 highlighting amino acids participating in the dimer interface. Residues in the dimer interfaces where amino acids are within 4 Å of the other chain in the corresponding structures are highlighted in purple (EBOV) and orange (RESTV).

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 70| Part 4| March 2014| Pages 457-460

doi:10.1107/S2053230X14003811

Follow Acta Cryst. F

Search term		doi		Advanced search
Author		volume	page