 |
PDBsum entry 1uw7
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Viral protein
|
PDB id
|
|
|
|
1uw7
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The nsp9 replicase protein of sars-Coronavirus, Structure and functional insights.
|
|
|
Authors
|
|
G.Sutton,
E.Fry,
L.Carter,
S.Sainsbury,
T.Walter,
J.Nettleship,
N.Berrow,
R.Owens,
R.Gilbert,
A.Davidson,
S.Siddell,
L.L.Poon,
J.Diprose,
D.Alderton,
M.Walsh,
J.M.Grimes,
D.I.Stuart.
|
|
|
Ref.
|
|
Structure, 2004,
12,
341-353.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
As part of a high-throughput structural analysis of SARS-coronavirus (SARS-CoV)
proteins, we have solved the structure of the non-structural protein 9 (nsp9).
This protein, encoded by ORF1a, has no designated function but is most likely
involved with viral RNA synthesis. The protein comprises a single beta-barrel
with a fold previously unseen in single domain proteins. The fold superficially
resembles an OB-fold with a C-terminal extension and is related to both of the
two subdomains of the SARS-CoV 3C-like protease (which belongs to the serine
protease superfamily). nsp9 has, presumably, evolved from a protease. The
crystal structure suggests that the protein is dimeric. This is confirmed by
analytical ultracentrifugation and dynamic light scattering. We show that nsp9
binds RNA and interacts with nsp8, activities that may be essential for its
function(s).
|
|
|
|
|
|
Figure 1.
Figure 1. Structure of SARS-CoV nsp9(A) A stereo a carbon
trace colored blue to red from the N to the C terminus. The nine
residues of the N-terminal tag are shown dashed. Every tenth
residue is labeled.(B) A stereo ribbon depiction colored as in
(A) with the main secondary structure elements labeled according
to Figure 2C. The N-terminal tag residues are shown transparent.
Figures are produced using BOBSCRIPT (Esnouf, 1997) and RASTER3D
(Merrit and Murphy, 1994).(C) Stereo diagram of the 2F[o] - F[c]
electron density for the C-terminal a helix residues 101-111,
contoured at 1s. The electron density is shown as a green mesh
with the residues depicted in red ball-and-stick.
|
|
|
|
|
|
The above figure is
reprinted
by permission from Cell Press:
Structure
(2004,
12,
341-353)
copyright 2004.
|
|
|
|
|
|
|
