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PDBsum entry 1bv6
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Oxygen storage/transport
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PDB id
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1bv6
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DOI no:
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Proc Natl Acad Sci U S A
95:15177-15182
(1998)
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PubMed id:
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Structure of a biological oxygen sensor: a new mechanism for heme-driven signal transduction.
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W.Gong,
B.Hao,
S.S.Mansy,
G.Gonzalez,
M.A.Gilles-Gonzalez,
M.K.Chan.
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ABSTRACT
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The FixL proteins are biological oxygen sensors that restrict the expression of
specific genes to hypoxic conditions. FixL's oxygen-detecting domain is a heme
binding region that controls the activity of an attached histidine kinase. The
FixL switch is regulated by binding of oxygen and other strong-field ligands. In
the absence of bound ligand, the heme domain permits kinase activity. In the
presence of bound ligand, this domain turns off kinase activity. Comparison of
the structures of two forms of the Bradyrhizobium japonicum FixL heme domain,
one in the "on" state without bound ligand and one in the
"off" state with bound cyanide, reveals a mechanism of regulation by a
heme that is distinct from the classical hemoglobin models. The close structural
resemblance of the FixL heme domain to the photoactive yellow protein confirms
the existence of a PAS structural motif but reveals the presence of an
alternative regulatory gateway.
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Selected figure(s)
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Figure 3.
Fig. 3. Ball-and-stick diagrams of three heme-binding
pockets. Structures are shown for Glycera dibranchiata
hemoglobin (PDB ID: 2HBG) (Left), BjFixLH (Center), and the NO
transporter protein (PDB ID: 1NP1) (Right) (27, 28). The
rightmost and leftmost side chains correspond to the E7 and E11
residues of hemoglobins, respectively. The additional side chain
in BjFixLH (red) corresponds to Ile 215. The structures were
aligned based on the orientation of the proximal histidine and
the porphyrin ring. The atoms are colored as in Fig. 1.
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Figure 5.
Fig. 5. Comparison of the structures of the regulatory FG
loop of BjFixLH in the unliganded "on" and cyanide bound "off"
states. (A) The structure of the FG loop in the met-BjFixLH
(brown) illustrating the hydrogen-bonding interactions (Left)
and 2F[O]-F[C] electron density map (1 ) (Right).
(B) Corresponding figure for cyanomet-BjFixLH (blue) showing
hydrogen bonding (Left) and electron density (Right). (C)
Stereoview of overlap of the refined models for both states.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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B.Goblirsch,
R.C.Kurker,
B.R.Streit,
C.M.Wilmot,
and
J.L.DuBois
(2011).
Chlorite dismutases, DyPs, and EfeB: 3 microbial heme enzyme families comprise the CDE structural superfamily.
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J Mol Biol,
408,
379-398.
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J.D.Satterlee
(2011).
Origins of aging mass loss in recombinant N-terminus and C-terminus deletion mutants of the heme-PAS biosensor domain BjFixLH(140-270).
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J Inorg Biochem,
105,
609-615.
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J.King-Scott,
P.V.Konarev,
S.Panjikar,
R.Jordanova,
D.I.Svergun,
and
P.A.Tucker
(2011).
Structural characterization of the multidomain regulatory protein Rv1364c from Mycobacterium tuberculosis.
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Structure,
19,
56-69.
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K.J.Watts,
B.L.Taylor,
and
M.S.Johnson
(2011).
PAS/poly-HAMP signalling in Aer-2, a soluble haem-based sensor.
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| |
Mol Microbiol,
79,
686-699.
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T.Drepper,
U.Krauss,
S.Meyer Zu Berstenhorst,
J.Pietruszka,
and
K.E.Jaeger
(2011).
Lights on and action! Controlling microbial gene expression by light.
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Appl Microbiol Biotechnol,
90,
23-40.
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A.J.Campbell,
K.J.Watts,
M.S.Johnson,
and
B.L.Taylor
(2010).
Gain-of-function mutations cluster in distinct regions associated with the signalling pathway in the PAS domain of the aerotaxis receptor, Aer.
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Mol Microbiol,
77,
575-586.
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J.Cheung,
and
W.A.Hendrickson
(2010).
Sensor domains of two-component regulatory systems.
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Curr Opin Microbiol,
13,
116-123.
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O.Torres-Quesada,
R.I.Oruezabal,
A.Peregrina,
E.Jofré,
J.Lloret,
R.Rivilla,
N.Toro,
and
J.I.Jiménez-Zurdo
(2010).
The Sinorhizobium meliloti RNA chaperone Hfq influences central carbon metabolism and the symbiotic interaction with alfalfa.
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BMC Microbiol,
10,
71.
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T.Yamashita
(2010).
[Recent studies on gas sensors, CooA, FixL, and Dos]
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Yakugaku Zasshi,
130,
1181-1187.
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H.Y.Cho,
H.J.Cho,
Y.M.Kim,
J.I.Oh,
and
B.S.Kang
(2009).
Structural insight into the heme-based redox sensing by DosS from Mycobacterium tuberculosis.
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J Biol Chem,
284,
13057-13067.
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PDB codes:
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J.Green,
J.C.Crack,
A.J.Thomson,
and
N.E.LeBrun
(2009).
Bacterial sensors of oxygen.
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Curr Opin Microbiol,
12,
145-151.
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M.D.Suits,
J.Lang,
G.P.Pal,
M.Couture,
and
Z.Jia
(2009).
Structure and heme binding properties of Escherichia coli O157:H7 ChuX.
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Protein Sci,
18,
825-838.
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PDB code:
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M.R.Evans,
P.B.Card,
and
K.H.Gardner
(2009).
ARNT PAS-B has a fragile native state structure with an alternative beta-sheet register nearby in sequence space.
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Proc Natl Acad Sci U S A,
106,
2617-2622.
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PDB code:
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M.V.Navarro,
N.De,
N.Bae,
Q.Wang,
and
H.Sondermann
(2009).
Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX.
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Structure,
17,
1104-1116.
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PDB codes:
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R.Gao,
and
A.M.Stock
(2009).
Biological insights from structures of two-component proteins.
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Annu Rev Microbiol,
63,
133-154.
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S.Yamada,
H.Sugimoto,
M.Kobayashi,
A.Ohno,
H.Nakamura,
and
Y.Shiro
(2009).
Structure of PAS-linked histidine kinase and the response regulator complex.
|
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Structure,
17,
1333-1344.
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PDB codes:
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T.H.Scheuermann,
D.R.Tomchick,
M.Machius,
Y.Guo,
R.K.Bruick,
and
K.H.Gardner
(2009).
Artificial ligand binding within the HIF2alpha PAS-B domain of the HIF2 transcription factor.
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Proc Natl Acad Sci U S A,
106,
450-455.
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PDB codes:
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T.Senda,
M.Senda,
S.Kimura,
and
T.Ishida
(2009).
Redox control of protein conformation in flavoproteins.
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Antioxid Redox Signal,
11,
1741-1766.
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Y.W.He,
C.Boon,
L.Zhou,
and
L.H.Zhang
(2009).
Co-regulation of Xanthomonas campestris virulence by quorum sensing and a novel two-component regulatory system RavS/RavR.
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Mol Microbiol,
71,
1464-1476.
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C.Olea,
E.M.Boon,
P.Pellicena,
J.Kuriyan,
and
M.A.Marletta
(2008).
Probing the function of heme distortion in the H-NOX family.
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ACS Chem Biol,
3,
703-710.
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PDB code:
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J.M.Lee,
H.Y.Cho,
H.J.Cho,
I.J.Ko,
S.W.Park,
H.S.Baik,
J.H.Oh,
C.Y.Eom,
Y.M.Kim,
B.S.Kang,
and
J.I.Oh
(2008).
O2- and NO-sensing mechanism through the DevSR two-component system in Mycobacterium smegmatis.
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J Bacteriol,
190,
6795-6804.
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PDB codes:
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K.J.Watts,
M.S.Johnson,
and
B.L.Taylor
(2008).
Structure-function relationships in the HAMP and proximal signaling domains of the aerotaxis receptor Aer.
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J Bacteriol,
190,
2118-2127.
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L.M.Podust,
A.Ioanoviciu,
and
P.R.Ortiz de Montellano
(2008).
2.3 A X-ray structure of the heme-bound GAF domain of sensory histidine kinase DosT of Mycobacterium tuberculosis.
|
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Biochemistry,
47,
12523-12531.
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PDB code:
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R.A.Ayers,
and
K.Moffat
(2008).
Changes in quaternary structure in the signaling mechanisms of PAS domains.
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Biochemistry,
47,
12078-12086.
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PDB codes:
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R.L.Kerby,
H.Youn,
and
G.P.Roberts
(2008).
RcoM: a new single-component transcriptional regulator of CO metabolism in bacteria.
|
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J Bacteriol,
190,
3336-3343.
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S.Mesa,
F.Hauser,
M.Friberg,
E.Malaguti,
H.M.Fischer,
and
H.Hennecke
(2008).
Comprehensive assessment of the regulons controlled by the FixLJ-FixK2-FixK1 cascade in Bradyrhizobium japonicum.
|
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J Bacteriol,
190,
6568-6579.
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A.Ioanoviciu,
E.T.Yukl,
P.Moënne-Loccoz,
and
P.R.de Montellano
(2007).
DevS, a heme-containing two-component oxygen sensor of Mycobacterium tuberculosis.
|
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Biochemistry,
46,
4250-4260.
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A.Möglich,
and
K.Moffat
(2007).
Structural basis for light-dependent signaling in the dimeric LOV domain of the photosensor YtvA.
|
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J Mol Biol,
373,
112-126.
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PDB codes:
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A.Pandini,
M.S.Denison,
Y.Song,
A.A.Soshilov,
and
L.Bonati
(2007).
Structural and functional characterization of the aryl hydrocarbon receptor ligand binding domain by homology modeling and mutational analysis.
|
| |
Biochemistry,
46,
696-708.
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|
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B.L.Taylor
(2007).
Aer on the inside looking out: paradigm for a PAS-HAMP role in sensing oxygen, redox and energy.
|
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Mol Microbiol,
65,
1415-1424.
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D.A.Landfried,
D.A.Vuletich,
M.P.Pond,
and
J.T.Lecomte
(2007).
Structural and thermodynamic consequences of b heme binding for monomeric apoglobins and other apoproteins.
|
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Gene,
398,
12-28.
|
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E.H.Sousa,
J.R.Tuckerman,
G.Gonzalez,
and
M.A.Gilles-Gonzalez
(2007).
DosT and DevS are oxygen-switched kinases in Mycobacterium tuberculosis.
|
| |
Protein Sci,
16,
1708-1719.
|
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G.Moro,
L.Bonati,
M.Bruschi,
U.Cosentino,
L.De Gioia,
P.C.Fantucci,
A.Pandini,
E.Papaleo,
D.Pitea,
G.A.Saracino,
and
G.Zampella
(2007).
Computational approaches to shed light on molecular mechanisms in biological processes.
|
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Theor Chem Acc,
117,
723-741.
|
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J.M.Christie
(2007).
Phototropin blue-light receptors.
|
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Annu Rev Plant Biol,
58,
21-45.
|
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V.Buttani,
A.Losi,
T.Eggert,
U.Krauss,
K.E.Jaeger,
Z.Cao,
and
W.Gärtner
(2007).
Conformational analysis of the blue-light sensing protein YtvA reveals a competitive interface for LOV-LOV dimerization and interdomain interactions.
|
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Photochem Photobiol Sci,
6,
41-49.
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K.J.Watts,
K.Sommer,
S.L.Fry,
M.S.Johnson,
and
B.L.Taylor
(2006).
Function of the N-terminal cap of the PAS domain in signaling by the aerotaxis receptor Aer.
|
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J Bacteriol,
188,
2154-2162.
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T.Mascher,
J.D.Helmann,
and
G.Unden
(2006).
Stimulus perception in bacterial signal-transducing histidine kinases.
|
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Microbiol Mol Biol Rev,
70,
910-938.
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A.Brencic,
and
S.C.Winans
(2005).
Detection of and response to signals involved in host-microbe interactions by plant-associated bacteria.
|
| |
Microbiol Mol Biol Rev,
69,
155-194.
|
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O.Yildiz,
M.Doi,
I.Yujnovsky,
L.Cardone,
A.Berndt,
S.Hennig,
S.Schulze,
C.Urbanke,
P.Sassone-Corsi,
and
E.Wolf
(2005).
Crystal structure and interactions of the PAS repeat region of the Drosophila clock protein PERIOD.
|
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Mol Cell,
17,
69-82.
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PDB code:
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S.Crosson,
P.T.McGrath,
C.Stephens,
H.H.McAdams,
and
L.Shapiro
(2005).
Conserved modular design of an oxygen sensory/signaling network with species-specific output.
|
| |
Proc Natl Acad Sci U S A,
102,
8018-8023.
|
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S.Mesa,
Z.Ucurum,
H.Hennecke,
and
H.M.Fischer
(2005).
Transcription activation in vitro by the Bradyrhizobium japonicum regulatory protein FixK2.
|
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J Bacteriol,
187,
3329-3338.
|
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A.Baruah,
B.Lindsey,
Y.Zhu,
and
M.M.Nakano
(2004).
Mutational analysis of the signal-sensing domain of ResE histidine kinase from Bacillus subtilis.
|
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J Bacteriol,
186,
1694-1704.
|
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E.Nagababu,
and
J.M.Rifkind
(2004).
Heme degradation by reactive oxygen species.
|
| |
Antioxid Redox Signal,
6,
967-978.
|
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|
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G.Alexandre,
S.Greer-Phillips,
and
I.B.Zhulin
(2004).
Ecological role of energy taxis in microorganisms.
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| |
FEMS Microbiol Rev,
28,
113-126.
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G.P.Roberts,
H.Youn,
and
R.L.Kerby
(2004).
CO-sensing mechanisms.
|
| |
Microbiol Mol Biol Rev,
68,
453-473.
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|
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H.Youn,
R.L.Kerby,
M.Conrad,
and
G.P.Roberts
(2004).
Functionally critical elements of CooA-related CO sensors.
|
| |
J Bacteriol,
186,
1320-1329.
|
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|
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J.Green,
and
M.S.Paget
(2004).
Bacterial redox sensors.
|
| |
Nat Rev Microbiol,
2,
954-966.
|
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|
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L.Rickman,
J.W.Saldanha,
D.M.Hunt,
D.N.Hoar,
M.J.Colston,
J.B.Millar,
and
R.S.Buxton
(2004).
A two-component signal transduction system with a PAS domain-containing sensor is required for virulence of Mycobacterium tuberculosis in mice.
|
| |
Biochem Biophys Res Commun,
314,
259-267.
|
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M.H.Hefti,
K.J.Françoijs,
S.C.de Vries,
R.Dixon,
and
J.Vervoort
(2004).
The PAS fold. A redefinition of the PAS domain based upon structural prediction.
|
| |
Eur J Biochem,
271,
1198-1208.
|
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|
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P.Pellicena,
D.S.Karow,
E.M.Boon,
M.A.Marletta,
and
J.Kuriyan
(2004).
Crystal structure of an oxygen-binding heme domain related to soluble guanylate cyclases.
|
| |
Proc Natl Acad Sci U S A,
101,
12854-12859.
|
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PDB codes:
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R.J.Kewley,
M.L.Whitelaw,
and
A.Chapman-Smith
(2004).
The mammalian basic helix-loop-helix/PAS family of transcriptional regulators.
|
| |
Int J Biochem Cell Biol,
36,
189-204.
|
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|
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R.Paul,
S.Weiser,
N.C.Amiot,
C.Chan,
T.Schirmer,
B.Giese,
and
U.Jenal
(2004).
Cell cycle-dependent dynamic localization of a bacterial response regulator with a novel di-guanylate cyclase output domain.
|
| |
Genes Dev,
18,
715-727.
|
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|
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S.Herrmann,
Q.Ma,
M.S.Johnson,
A.V.Repik,
and
B.L.Taylor
(2004).
PAS domain of the Aer redox sensor requires C-terminal residues for native-fold formation and flavin adenine dinucleotide binding.
|
| |
J Bacteriol,
186,
6782-6791.
|
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|
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U.Jenal
(2004).
Cyclic di-guanosine-monophosphate comes of age: a novel secondary messenger involved in modulating cell surface structures in bacteria?
|
| |
Curr Opin Microbiol,
7,
185-191.
|
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|
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C.M.Dunham,
E.M.Dioum,
J.R.Tuckerman,
G.Gonzalez,
W.G.Scott,
and
M.A.Gilles-Gonzalez
(2003).
A distal arginine in oxygen-sensing heme-PAS domains is essential to ligand binding, signal transduction, and structure.
|
| |
Biochemistry,
42,
7701-7708.
|
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PDB code:
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|
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K.Saito,
E.Ito,
K.Hosono,
K.Nakamura,
K.Imai,
T.Iizuka,
Y.Shiro,
and
H.Nakamura
(2003).
The uncoupling of oxygen sensing, phosphorylation signalling and transcriptional activation in oxygen sensor FixL and FixJ mutants.
|
| |
Mol Microbiol,
48,
373-383.
|
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|
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|
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L.M.Iyer,
V.Anantharaman,
and
L.Aravind
(2003).
Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins.
|
| |
BMC Genomics,
4,
5.
|
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|
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M.A.Cusanovich,
and
T.E.Meyer
(2003).
Photoactive yellow protein: a prototypic PAS domain sensory protein and development of a common signaling mechanism.
|
| |
Biochemistry,
42,
4759-4770.
|
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|
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P.Geigenberger
(2003).
Response of plant metabolism to too little oxygen.
|
| |
Curr Opin Plant Biol,
6,
247-256.
|
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|
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|
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P.J.Erbel,
P.B.Card,
O.Karakuzu,
R.K.Bruick,
and
K.H.Gardner
(2003).
Structural basis for PAS domain heterodimerization in the basic helix--loop--helix-PAS transcription factor hypoxia-inducible factor.
|
| |
Proc Natl Acad Sci U S A,
100,
15504-15509.
|
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PDB code:
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|
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U.Liebl,
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
|
');
}
}
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