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(+ 4 more)
41 a.a.
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(+ 4 more)
604 a.a.
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411 a.a.
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1284 a.a.
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1018 a.a.
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1154 a.a.
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* Residue conservation analysis
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PDB id:
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Virus
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Title:
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Atomic cryoem structure of a nonenveloped virus suggests how membrane penetration protein is primed for cell entry
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Structure:
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Outer capsid vp4. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q, r, s, t. Core protein vp6. Chain: u, v. Vp1. Chain: w. Vp3. Chain: x, y
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Source:
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Grass carp reovirus. Organism_taxid: 128987. Organism_taxid: 128987
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Authors:
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X.Zhang,L.Jin,Q.Fang,W.Hui,Z.H.Zhou
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Key ref:
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X.Zhang
et al.
(2010).
3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry.
Cell,
141,
472-482.
PubMed id:
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Date:
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02-Feb-10
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Release date:
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12-May-10
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PROCHECK
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Headers
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References
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Cell
141:472-482
(2010)
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PubMed id:
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3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry.
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X.Zhang,
L.Jin,
Q.Fang,
W.H.Hui,
Z.H.Zhou.
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ABSTRACT
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To achieve cell entry, many nonenveloped viruses must transform from a dormant
to a primed state. In contrast to the membrane fusion mechanism of enveloped
viruses (e.g., influenza virus), this membrane penetration mechanism is poorly
understood. Here, using single-particle cryo-electron microscopy, we report a
3.3 A structure of the primed, infectious subvirion particle of aquareovirus.
The density map reveals side-chain densities of all types of amino acids (except
glycine), enabling construction of a full-atom model of the viral particle. Our
structure and biochemical results show that priming involves autocleavage of the
membrane penetration protein and suggest that Lys84 and Glu76 may facilitate
this autocleavage in a nucleophilic attack. We observe a myristoyl group,
covalently linked to the N terminus of the penetration protein and embedded in a
hydrophobic pocket. These results suggest a well-orchestrated process of
nonenveloped virus entry involving autocleavage of the penetration protein prior
to exposure of its membrane-insertion finger.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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Y.Mao,
L.Wang,
C.Gu,
A.Herschhorn,
S.H.Xiang,
H.Haim,
X.Yang,
and
J.Sodroski
(2012).
Subunit organization of the membrane-bound HIV-1 envelope glycoprotein trimer.
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Nat Struct Mol Biol,
19,
893-899.
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E.C.Settembre,
J.Z.Chen,
P.R.Dormitzer,
N.Grigorieff,
and
S.C.Harrison
(2011).
Atomic model of an infectious rotavirus particle.
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EMBO J,
30,
408-416.
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PDB codes:
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L.Cheng,
J.Sun,
K.Zhang,
Z.Mou,
X.Huang,
G.Ji,
F.Sun,
J.Zhang,
and
P.Zhu
(2011).
Atomic model of a cypovirus built from cryo-EM structure provides insight into the mechanism of mRNA capping.
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Proc Natl Acad Sci U S A,
108,
1373-1378.
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PDB code:
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M.Karuppasamy,
F.Karimi Nejadasl,
M.Vulovic,
A.J.Koster,
and
R.B.Ravelli
(2011).
Radiation damage in single-particle cryo-electron microscopy: effects of dose and dose rate.
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J Synchrotron Radiat,
18,
398-412.
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M.L.Baker,
S.S.Abeysinghe,
S.Schuh,
R.A.Coleman,
A.Abrams,
M.P.Marsh,
C.F.Hryc,
T.Ruths,
W.Chiu,
and
T.Ju
(2011).
Modeling protein structure at near atomic resolutions with Gorgon.
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J Struct Biol,
174,
360-373.
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N.Grigorieff,
and
S.C.Harrison
(2011).
Near-atomic resolution reconstructions of icosahedral viruses from electron cryo-microscopy.
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Curr Opin Struct Biol,
21,
265-273.
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R.M.Glaeser,
D.Typke,
P.C.Tiemeijer,
J.Pulokas,
and
A.Cheng
(2011).
Precise beam-tilt alignment and collimation are required to minimize the phase error associated with coma in high-resolution cryo-EM.
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J Struct Biol,
174,
1.
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S.A.Claridge,
J.J.Schwartz,
and
P.S.Weiss
(2011).
Electrons, photons, and force: quantitative single-molecule measurements from physics to biology.
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ACS Nano,
5,
693-729.
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K.Lasker,
A.Sali,
and
H.J.Wolfson
(2010).
Determining macromolecular assembly structures by molecular docking and fitting into an electron density map.
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Proteins,
78,
3205-3211.
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T.Fujii,
A.H.Iwane,
T.Yanagida,
and
K.Namba
(2010).
Direct visualization of secondary structures of F-actin by electron cryomicroscopy.
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Nature,
467,
724-728.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
