 |
PDBsum entry 6w2d
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Viral protein
|
PDB id
|
|
|
|
6w2d
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
1352 a.a.
|
|
|
|
|
|
|
|
|
|
|
1283 a.a.
|
|
|
|
|
|
|
|
|
|
|
292 a.a.
|
|
|
|
|
|
|
|
|
|
|
68 a.a.
|
|
|
|
|
|
|
|
|
|
|
37 a.a.
|
|
|
|
|
|
|
|
|
|
|
77 a.a.
|
|
|
|
|
|
|
|
|
|
|
63 a.a.
|
|
|
|
|
|
|
|
|
|
|
315 a.a.
|
|
|
|
|
|
|
|
|
|
|
336 a.a.
|
|
|
|
|
|
|
|
|
|
|
299 a.a.
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structures of capsid and capsid-Associated tegument complex inside the epstein-Barr virus.
|
|
|
Authors
|
|
W.Liu,
Y.Cui,
C.Wang,
Z.Li,
D.Gong,
X.Dai,
G.Q.Bi,
R.Sun,
Z.H.Zhou.
|
|
|
Ref.
|
|
Nat Microbiol, 2020,
5,
1285-1298.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
|
|
|
Abstract
|
|
|
As the first discovered human cancer virus, Epstein-Barr virus (EBV) causes
Burkitt's lymphoma and nasopharyngeal carcinoma. Isolating virions for
determining high-resolution structures has been hindered by latency-a hallmark
of EBV infection-and atomic structures are thus available only for recombinantly
expressed EBV proteins. In the present study, by symmetry relaxation and
subparticle reconstruction, we have determined near-atomic-resolution structures
of the EBV capsid with an asymmetrically attached DNA-translocating portal and
capsid-associated tegument complexes from cryogenic electron microscopy images
of just 2,048 EBV virions obtained by chemical induction. The resulting atomic
models reveal structural plasticity among the 20 conformers of the major capsid
protein, 2 conformers of the small capsid protein (SCP), 4 conformers of the
triplex monomer proteins and 2 conformers of the triplex dimer proteins.
Plasticity reaches the greatest level at the capsid-tegument interfaces
involving SCP and capsid-associated tegument complexes (CATC): SCPs crown
pentons/hexons and mediate tegument protein binding, and CATCs bind and rotate
all five periportal triplexes, but notably only about one peri-penton triplex.
These results offer insights into the EBV capsid assembly and a mechanism for
recruiting cell-regulating factors into the tegument compartment as 'cargoes',
and should inform future anti-EBV strategies.
|
|
|
|
|
|
|
