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PDBsum entry 1h2c
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Virus/viral protein
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PDB id
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1h2c
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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The matrix protein vp40 from ebola virus octamerizes into pore-Like structures with specific RNA binding properties.
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Authors
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F.X.Gomis-Rüth,
A.Dessen,
J.Timmins,
A.Bracher,
L.Kolesnikowa,
S.Becker,
H.D.Klenk,
W.Weissenhorn.
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Ref.
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Structure, 2003,
11,
423-433.
[DOI no: ]
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PubMed id
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Abstract
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The Ebola virus membrane-associated matrix protein VP40 is thought to be crucial
for assembly and budding of virus particles. Here we present the crystal
structure of a disk-shaped octameric form of VP40 formed by four antiparallel
homodimers of the N-terminal domain. The octamer binds an RNA triribonucleotide
containing the sequence 5'-U-G-A-3' through its inner pore surface, and its
oligomerization and RNA binding properties are facilitated by two conformational
changes when compared to monomeric VP40. The selective RNA interaction
stabilizes the ring structure and confers in vitro SDS resistance to octameric
VP40. SDS-resistant octameric VP40 is also found in Ebola virus-infected cells,
which suggests that VP40 has an additional function in the life cycle of the
virus besides promoting virus assembly and budding off the plasma membrane.
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Figure 4.
Figure 4. Comparison of the NTDs Derived from the Closed
Monomeric Conformation and from the Ring Structure Unveils Major
Conformational Changes(A) Superposition of Ca atoms 71 to 191
results in an rms deviation of 2.8 Å. Sites of major
conformational movements are indicated with arrows. The NTD from
the closed monomeric conformation is shown in red and the one
from the octamer structure in yellow.(B) Schematic overview of
the two major conformational changes in VP40. An N-terminal loop
(gray) and the C-terminal domain (gray) from the closed VP40
conformation must change their conformation to achieve
octamerization. This is indicated by the ribbon drawing of the
three regions involved; the potential movement of the two
domains with respect to the N-terminal domain is highlighted by
arrows.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2003,
11,
423-433)
copyright 2003.
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Secondary reference #1
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Title
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Crystal structure of the matrix protein vp40 from ebola virus.
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Authors
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A.Dessen,
V.Volchkov,
O.Dolnik,
H.D.Klenk,
W.Weissenhorn.
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Ref.
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EMBO J, 2000,
19,
4228-4236.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1 Stereo view of the experimental map generated with MAD
phases obtained from six selenium sites identified by SOLVE and
subsequently solvent flattened. The map is contoured at the 1
 level,
and focuses on a conserved loop region in domain 2 connecting
 -strands
7 and 8.
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Figure 4.
Figure 4 Interdomain interactions. (A) Close up of polar
interactions between the N- and C-terminal domains. Residues
involved in salt bridges and hydrogen bonds are shown. For
clarity, the connection between residue 307 and 310 is shown as
a grey dashed line. The loop connecting both domains is
indicated with an arrow. (B) Surface representation of the
N-terminal domain (residues 44–194) and (C) of the C-terminal
domain (residues 201–321). Hydrophobic residues lining the
interface on the N- and C-terminal domains are shown in green.
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The above figures are
reproduced from the cited reference
which is an Open Access publication published by Macmillan Publishers Ltd
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