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PDBsum entry 1vio
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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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Structure of the pseudouridine synthase rsua from haemophilus influenzae.
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Authors
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A.Matte,
G.V.Louie,
J.Sivaraman,
M.Cygler,
S.K.Burley.
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Ref.
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Acta Crystallograph Sect F Struct Biol Cryst Commun, 2005,
61,
350-354.
[DOI no: ]
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PubMed id
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Abstract
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The structure of the pseudouridine synthase RsuA from Haemophilus influenza,
which catalyzes the conversion of uridine to pseudouridine at a single position
within 16S ribosomal RNA, has been determined at 1.59 A resolution and compared
with that of Escherichia coli RsuA. The H. influenza enzyme contains an
N-terminal S4-like alpha3beta4 domain followed by a catalytic domain, as
observed in the structure of E. coli RsuA. Whereas the individual domains of E.
coli and H. influenza RsuA are structurally similar, their relative spatial
disposition differs greatly between the two structures. The former displays an
extended open conformation with no direct contacts between the domains, while
the latter is in a closed conformation with a large interface between the two
domains. Domain closure presents several basic and polar residues into a
putative RNA-binding cleft. It is proposed that this relative repositioning of
the S4 and catalytic domains is used to modulate the shape and size of the
rRNA-binding site in RsuA and in other pseudouridine synthases possessing S4
domains.
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Figure 1.
Figure 1 The structure of H. influenzae RsuA, showing the
head-to-tail orientation of both molecules comprising the
asymmetric unit. The two molecules are coloured blue and cyan or
yellow and green for the catalytic and  [3]
 [4]
S4 domains, respectively. The catalytic residue (Asp102, red) is
shown in atomic stick figure representation. The figure was
prepared using PyMol (DeLano, 2002[DeLano, W. L. (2002). The
PyMOL Molecular Graphics System, http://www.pymol.org .]).
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The above figure is
reprinted
from an Open Access publication published by the IUCr:
Acta Crystallograph Sect F Struct Biol Cryst Commun
(2005,
61,
350-354)
copyright 2005.
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Secondary reference #1
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Title
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Structural analysis of a set of proteins resulting from a bacterial genomics project.
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Authors
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J.Badger,
J.M.Sauder,
J.M.Adams,
S.Antonysamy,
K.Bain,
M.G.Bergseid,
S.G.Buchanan,
M.D.Buchanan,
Y.Batiyenko,
J.A.Christopher,
S.Emtage,
A.Eroshkina,
I.Feil,
E.B.Furlong,
K.S.Gajiwala,
X.Gao,
D.He,
J.Hendle,
A.Huber,
K.Hoda,
P.Kearins,
C.Kissinger,
B.Laubert,
H.A.Lewis,
J.Lin,
K.Loomis,
D.Lorimer,
G.Louie,
M.Maletic,
C.D.Marsh,
I.Miller,
J.Molinari,
H.J.Muller-Dieckmann,
J.M.Newman,
B.W.Noland,
B.Pagarigan,
F.Park,
T.S.Peat,
K.W.Post,
S.Radojicic,
A.Ramos,
R.Romero,
M.E.Rutter,
W.E.Sanderson,
K.D.Schwinn,
J.Tresser,
J.Winhoven,
T.A.Wright,
L.Wu,
J.Xu,
T.J.Harris.
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Ref.
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Proteins, 2005,
60,
787-796.
[DOI no: ]
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PubMed id
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Figure 1.
Figure 1. Ribbon diagrams[54] of the eleven structures
described in the Results and Discussion section: (A) monomer
from the dapE structure (1VGY), (B) homodimer from the nudE
structure (1VHG), (C) monomer from the DUS structure (1VHN), (D)
monomer from the ysdC structure, 1VHE, (E) monomer from the frwX
structure, 1VHO, (F) monomer from the perB structure (1VIZ), (G)
monomer from the plsX structure (1VI1), (H) monomer from the
yqgF structure (1VHX), (I) monomer from the yigZ structure
(1VI7), (J) monomer from the YiiM structure (1O65), (K) the
novel sufD structure (1VH4) with the homodimer interface in the
center.
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The above figure is
reproduced from the cited reference
with permission from John Wiley & Sons, Inc.
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