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PDBsum entry 2v4x
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Viral protein
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PDB id
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2v4x
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Contents |
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* Residue conservation analysis
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PDB id:
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Viral protein
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Title:
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Crystal structure of jaagsiekte sheep retrovirus capsid n-terminal domain
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Structure:
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Capsid protein p27. Chain: a. Fragment: n-terminal domain, residues 257-388. Synonym: jsrv capsid. Engineered: yes
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Source:
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Jaagsiekte sheep retrovirus. Organism_taxid: 11746. Expressed in: escherichia coli. Expression_system_taxid: 469008.
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Resolution:
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1.50Å
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R-factor:
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0.152
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R-free:
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0.185
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Authors:
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G.B.Mortuza,D.C.Goldstone,C.Pashley,L.F.Haire,M.Palmarini,W.R.Taylor, J.P.Stoye,I.A.Taylor
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Key ref:
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G.B.Mortuza
et al.
(2009).
Structure of the capsid amino-terminal domain from the betaretrovirus, jaagsiekte sheep retrovirus.
J Mol Biol,
386,
1179-1192.
PubMed id:
DOI:
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Date:
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30-Sep-08
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Release date:
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25-Nov-08
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PROCHECK
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Headers
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References
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P31622
(GAG_JSRV) -
Gag polyprotein from Sheep pulmonary adenomatosis virus
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Seq:
Struc:
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612 a.a.
131 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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DOI no:
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J Mol Biol
386:1179-1192
(2009)
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PubMed id:
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Structure of the capsid amino-terminal domain from the betaretrovirus, jaagsiekte sheep retrovirus.
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G.B.Mortuza,
D.C.Goldstone,
C.Pashley,
L.F.Haire,
M.Palmarini,
W.R.Taylor,
J.P.Stoye,
I.A.Taylor.
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ABSTRACT
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Jaagsiekte sheep retrovirus is a betaretrovirus and the causative agent of
pulmonary adenocarcinoma, a transmissible lung tumour of sheep. Here we report
the crystal structure of the capsid amino-terminal domain and examine the
self-association properties of Jaagsiekte sheep retrovirus capsid. We find that
the structure is remarkably similar to the amino-terminal domain of the
alpharetrovirus, avian leukosis virus, revealing a previously undetected
evolutionary similarity. Examination of capsid self-association suggests a mode
of assembly not driven by the strong capsid carboxy-terminal domain interactions
that characterise capsid assembly in the lentiviruses. Based on these data, we
propose this structure provides a model for the capsid of betaretroviruses
including the HML-2 family of endogenous human betaretroviruses.
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Selected figure(s)
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Figure 1.
Fig. 1. Crystal structure of the N-terminal domain of the
JSRV capsid. (a) A cartoon representation of the JSRV capsid
N-terminal domain, α-helices and β-strands are numbered. (b)
Cartoon representation of JSRV-NtD oriented at 90° to (a),
highlighting the α4–α6 loop.
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Figure 3.
Fig. 3. Ribbon view of α4 in the capsid N-terminal domains
of JSRV (a), RSV (b), HIV (c), MLV (d) and HTLV (e). The
functionally important arginine is indicated in each panel.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2009,
386,
1179-1192)
copyright 2009.
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Figures were
selected
by an automated process.
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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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K.Kono,
H.Song,
M.Yokoyama,
H.Sato,
T.Shioda,
and
E.E.Nakayama
(2010).
Multiple sites in the N-terminal half of simian immunodeficiency virus capsid protein contribute to evasion from rhesus monkey TRIM5α-mediated restriction.
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Retrovirology,
7,
72.
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P.Schuck
(2010).
On computational approaches for size-and-shape distributions from sedimentation velocity analytical ultracentrifugation.
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Eur Biophys J,
39,
1261-1275.
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G.D.Bailey,
J.K.Hyun,
A.K.Mitra,
and
R.L.Kingston
(2009).
Proton-linked dimerization of a retroviral capsid protein initiates capsid assembly.
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Structure,
17,
737-748.
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PDB codes:
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J.G.Purdy,
J.M.Flanagan,
I.J.Ropson,
and
R.C.Craven
(2009).
Retroviral capsid assembly: a role for the CA dimer in initiation.
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J Mol Biol,
389,
438-451.
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O.Pornillos,
B.K.Ganser-Pornillos,
B.N.Kelly,
Y.Hua,
F.G.Whitby,
C.D.Stout,
W.I.Sundquist,
C.P.Hill,
and
M.Yeager
(2009).
X-ray structures of the hexameric building block of the HIV capsid.
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Cell,
137,
1282-1292.
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PDB codes:
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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
