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PDBsum entry 2a0b
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Sensory transduction
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PDB id
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2a0b
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References listed in PDB file
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Key reference
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Title
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Refined structure of the histidine-Containing phosphotransfer (hpt) domain of the anaerobic sensor kinase arcb from escherichia coli at 1.57 a resolution.
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Authors
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M.Kato,
T.Mizuno,
T.Shimizu,
T.Hakoshima.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1999,
55,
1842-1849.
[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 were identified by an automated
search of PubMed on title and author
names, giving a
percentage match of
89%.
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Abstract
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The crystal structure of the histidine-containing phosphotransfer (HPt) domain
of the anaerobic sensor kinase ArcB from Escherichia coli has been refined to
1.57 A resolution, using the coordinates of the earlier 2.06 A structure as a
starting model. The final model contained 956 protein atoms, one zinc ion and
156 water molecules, with an R factor of 19.0%. The high-resolution
electron-density maps clearly revealed additional solvent molecules and seven
discrete rotamers in the protein side chains. One residue, Met755, was fully
buried but was able to occupy the space in the hydrophobic core by means of the
two-state conformation of its side chain. One water molecule was buried in the
protein core and contributed to the rigidity of the HPt domain, cooperating in
the coordination of the zinc ion.
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Figure 2.
Figure 2 Discrete rotamers with their electron densities. The
residues are shown as ball-and-stick models. The densities are
contoured at the 1.0  level.
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Figure 4.
Figure 4 Stereo diagram of the Zn2+-binding site and buried
water molecule. All residues are shown as ball-and-stick models,
with water molecules (W6 and W7) and the Zn2+ ion as spheres.
Dashed lines indicate hydrogen bonds or coordinations to Zn2+.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(1999,
55,
1842-1849)
copyright 1999.
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Secondary reference #1
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Title
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Insights into multistep phosphorelay from the crystal structure of the c-Terminal hpt domain of arcb.
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Authors
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M.Kato,
T.Mizuno,
T.Shimizu,
T.Hakoshima.
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Ref.
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Cell, 1997,
88,
717-723.
[DOI no: ]
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PubMed id
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Figure 4.
Figure 4. Helix Structure and Sequence Alignment of HPt
DomainsSide-view of helix D of the HPt domain of ArcB using a
ball-and-stick model with the 2F[o]-F[c] electron density map.
The imidazole ring makes a hydrogen bond to a water molecule (W).
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Figure 5.
Figure 5. Comparison of HPt and P1 DomainsStructural
comparison of the HPt domain of ArcB (right) and the P1 domain
of CheA (left). The main chain is drawn as a ribbon in red for
helices D and E of the HPt domain of ArcB and the corresponding
part of CheA. The side chain of active His-717 of the HPt domain
and the location of the corresponding histidine in the P1 domain
are shown in green.
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The above figures are
reproduced from the cited reference
with permission from Cell Press
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Secondary reference #2
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Title
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Crystallization and preliminary X-Ray analysis of a histidine kinase domain of the anaerobic sensor protein arcb from escherichia coli.
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Authors
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M.Kato,
K.Ishige,
T.Mizuno,
T.Shimizu,
T.Hakoshima.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1996,
52,
1214-1215.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1. Crystal of ArcB
c. The scale bar is 0.5 mm long.
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The above figure is
reproduced from the cited reference
with permission from the IUCr
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