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PDBsum entry 2vqp
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Viral protein
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PDB id
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2vqp
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References listed in PDB file
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Key reference
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Title
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Surface features of a mononegavirales matrix protein indicate sites of membrane interaction.
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Authors
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V.A.Money,
H.K.Mcphee,
J.A.Mosely,
J.M.Sanderson,
R.P.Yeo.
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Ref.
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Proc Natl Acad Sci U S A, 2009,
106,
4441-4446.
[DOI no: ]
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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The matrix protein (M) of respiratory syncytial virus (RSV), the prototype viral
member of the Pneumovirinae (family Paramyxoviridae, order Mononegavirales), has
been crystallized and the structure determined to a resolution of 1.6 A. The
structure comprises 2 compact beta-rich domains connected by a relatively
unstructured linker region. Due to the high degree of side-chain order in the
structure, an extensive contiguous area of positive surface charge covering
approximately 600 A(2) can be resolved. This unusually large patch of positive
surface potential spans both domains and the linker, and provides a mechanism
for driving the interaction of the protein with a negatively-charged membrane
surface or other virion components such as the nucleocapsid. This patch is
complemented by regions of high hydrophobicity and a striking planar arrangement
of tyrosine residues encircling the C-terminal domain. Comparison of the RSV M
sequence with other members of the Pneumovirinae shows that regions of
divergence correspond to surface exposed loops in the M structure, with the
majority of viral species-specific differences occurring in the N-terminal
domain.
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Figure 2.
Comparison of the RSV M protein topology with that of EBOV
VP40. The diagrams show an overlay of the β-sheet arrangements
of M^254R with EBOV VP40 (PDB code 1ES6). (A) RSV M protein
N-terminal domain in blue and VP40 in yellow; and (B) M^254R
protein C-terminal domain in red and VP40 in cyan. The same
images are presented in Fig. S2, in stereoscopic views.
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Figure 5.
Distribution of tyrosine residues in the C-terminal domain of
the RSV M. The N-terminal domain of M^254R has been omitted for
clarity. The planar distribution of the residues (shown as
ball-and-stick representations) on the surface of the M protein
is readily apparent. The C-terminal residue is indicated by C; A
and B show orthogonal views of this domain.
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