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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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A structural genomics approach to the study of quorum sensing: crystal structures of three luxs orthologs.
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Authors
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H.A.Lewis,
E.B.Furlong,
B.Laubert,
G.A.Eroshkina,
Y.Batiyenko,
J.M.Adams,
M.G.Bergseid,
C.D.Marsh,
T.S.Peat,
W.E.Sanderson,
J.M.Sauder,
S.G.Buchanan.
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Ref.
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Structure, 2001,
9,
527-537.
[DOI no: ]
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PubMed id
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Abstract
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BACKGROUND: Quorum sensing is the mechanism by which bacteria control gene
expression in response to cell density. Two major quorum-sensing systems have
been identified, system 1 and system 2, each with a characteristic signaling
molecule (autoinducer-1, or AI-1, in the case of system 1, and AI-2 in system
2). The luxS gene is required for the AI-2 system of quorum sensing. LuxS and
AI-2 have been described in both Gram-negative and Gram-positive bacterial
species and have been shown to be involved in the expression of virulence genes
in several pathogens. RESULTS: The structure of the LuxS protein from three
different bacterial species with resolutions ranging from 1.8 A to 2.4 A has
been solved using an X-ray crystallographic structural genomics approach. The
structure of LuxS reported here is seen to have a new alpha-beta fold. In all
structures, an equivalent homodimer is observed. A metal ion identified as zinc
was seen bound to a Cys-His-His triad. Methionine was found bound to the protein
near the metal and at the dimer interface. CONCLUSIONS: These structures provide
support for a hypothesis that explains the in vivo action of LuxS. Specifically,
acting as a homodimer, the protein binds a methionine analog,
S-ribosylhomocysteine (SRH). The zinc atom is in position to cleave the ribose
ring in a step along the synthesis pathway of AI-2.
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Figure 6.
Figure 6. Ball and Stick and Ribbon Diagram of the
Substrate and Metal Binding SitesPotential hydrogen-bonding
partners for the methionine ligand are shown by white dotted
lines. Potential hydrogen bonding interactions with the zinc
atom are also shown
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2001,
9,
527-537)
copyright 2001.
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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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