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PDBsum entry 4jnh
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Viral protein
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PDB id
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4jnh
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PDB id:
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| Name: |
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Viral protein
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Title:
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A unique spumavirus gag n-terminal domain with functional properties of orthoretroviral matrix and capsid
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Structure:
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Gag polyprotein. Chain: a, b. Synonym: pr71gag, gag protein, p68gag, p3, p3gag. Engineered: yes
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Source:
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Human spumaretrovirus. Sfvcpz(hu). Organism_taxid: 11963. Gene: gag. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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2.40Å
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R-factor:
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0.175
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R-free:
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0.230
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Authors:
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I.A.Taylor,D.C.Goldstone,T.G.Flower,N.J.Ball
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Key ref:
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D.C.Goldstone
et al.
(2013).
A unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsid.
Plos Pathog,
9,
e1003376.
PubMed id:
DOI:
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Date:
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15-Mar-13
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Release date:
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29-May-13
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PROCHECK
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Headers
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References
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P14349
(GAG_FOAMV) -
Gag polyprotein from Human spumaretrovirus
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Seq:
Struc:
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648 a.a.
171 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 1 residue position (black
cross)
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DOI no:
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Plos Pathog
9:e1003376
(2013)
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PubMed id:
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A unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsid.
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D.C.Goldstone,
T.G.Flower,
N.J.Ball,
M.Sanz-Ramos,
M.W.Yap,
R.W.Ogrodowicz,
N.Stanke,
J.Reh,
D.Lindemann,
J.P.Stoye,
I.A.Taylor.
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ABSTRACT
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The Spumaretrovirinae, or foamyviruses (FVs) are complex retroviruses that
infect many species of monkey and ape. Although FV infection is apparently
benign, trans-species zoonosis is commonplace and has resulted in the isolation
of the Prototypic Foamy Virus (PFV) from human sources and the potential for
germ-line transmission. Despite little sequence homology, FV and orthoretroviral
Gag proteins perform equivalent functions, including genome packaging, virion
assembly, trafficking and membrane targeting. In addition, PFV Gag interacts
with the FV Envelope (Env) protein to facilitate budding of infectious
particles. Presently, there is a paucity of structural information with regards
FVs and it is unclear how disparate FV and orthoretroviral Gag molecules share
the same function. Therefore, in order to probe the functional overlap of FV and
orthoretroviral Gag and learn more about FV egress and replication we have
undertaken a structural, biophysical and virological study of PFV-Gag. We
present the crystal structure of a dimeric amino terminal domain from PFV,
Gag-NtD, both free and in complex with the leader peptide of PFV Env. The
structure comprises a head domain together with a coiled coil that forms the
dimer interface and despite the shared function it is entirely unrelated to
either the capsid or matrix of Gag from other retroviruses. Furthermore, we
present structural, biochemical and virological data that reveal the molecular
details of the essential Gag-Env interaction and in addition we also examine the
specificity of Trim5α restriction of PFV. These data provide the first
information with regards to FV structural proteins and suggest a model for
convergent evolution of gag genes where structurally unrelated molecules have
become functionally equivalent.
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Links
