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PDBsum entry 3us6
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References listed in PDB file
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Key reference
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Title
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Medicago truncatula histidine-Containing phosphotransfer protein: structural and biochemical insights into the cytokinin transduction pathway in plants.
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Authors
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M.Ruszkowski,
K.Brzezinski,
R.Jedrzejczak,
M.Dauter,
Z.Dauter,
M.Sikorski,
M.Jaskolski.
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Ref.
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Febs J, 2013,
280,
3709-3720.
[DOI no: ]
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PubMed id
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Abstract
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No abstract given.
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Secondary reference #1
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Title
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The arabidopsis histidine phosphotransfer proteins are redundant positive regulators of cytokinin signaling.
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Authors
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C.E.Hutchison,
J.Li,
C.Argueso,
M.Gonzalez,
E.Lee,
M.W.Lewis,
B.B.Maxwell,
T.D.Perdue,
G.E.Schaller,
J.M.Alonso,
J.R.Ecker,
J.J.Kieber.
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Ref.
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Plant Cell, 2006,
18,
3073-3087.
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PubMed id
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Secondary reference #2
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Title
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Crystal structure of the histidine-Containing phosphotransfer protein zmhp2 from maize.
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Authors
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H.Sugawara,
Y.Kawano,
T.Hatakeyama,
T.Yamaya,
N.Kamiya,
H.Sakakibara.
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Ref.
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Protein Sci, 2005,
14,
202-208.
[DOI no: ]
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PubMed id
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Figure 3.
Figure 3. Superimposition of active site structures of
ZmHP2 and YPD1. Helices D and E, their connecting loops of ZmHP2
(all in purple), and the corresponding regions of YPD1 (pink)
are shown. Oxygen, nitrogen, and sulfur atoms of selected
residues are shown in red, blue, and green, respectively.
Hydrogen bonds and salt bridges are indicated by dots.
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Figure 5.
Figure 5. Structural differences between ZmHP2 molecules in
the asymmetric unit around the loop connecting the four-helix
bundle with the N-terminal helices. Compared to Figure 1 Go- , this
figure is rotated by 90 degrees around the horizontal axis.
Since the structures of the monomers of each pair of ZmHP2
molecules in the asymmetric unit are essentially the same, only
molecules A1 (green) and B1 (purple) are shown. Oxygen, nitrogen
and sulfur atoms are shown in red, blue and green, respectively.
Hydrogen bonds and salt bridges are indicated by dots. In
molecule A1, residues 35-38 are indicated in yellow. Gly41 in
molecule A1 and three glycine residues (37, 38, and 41) in
molecule B1 are colored pink. The residues of molecule A1
involved in packing interactions with molecule B1 in the crystal
are shown in cyan.
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The above figures are
reproduced from the cited reference
with permission from the Protein Society
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Secondary reference #3
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Title
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Conservation of structure and function among histidine-Containing phosphotransfer (hpt) domains as revealed by the crystal structure of ypd1.
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Authors
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Q.Xu,
A.H.West.
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Ref.
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J Mol Biol, 1999,
292,
1039-1050.
[DOI no: ]
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PubMed id
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Figure 3.
Figure 3. A ribbon representation of the YPD1 structure.
The helices are numbered sequentially A to G from the N terminus
to the C terminus. The four-helix bundle core is composed of
helices B, C, D and G.
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Figure 5.
Figure 5. Sequence alignment of the aC-aD region of YPD1
with other HPt domains. Shown above the sequence alignment, is
the 2 ° structure alignment of the aC and aD helices of YPD1
that we believe form the binding/recognition surface for
response regulator domains. The numbering scheme across the top
of the sequence alignment refers to positions of residues
relative to the active-site histidine residue. The numbers in
the second column refer to the position of the active-site
histidine residue with respect to the primary sequence. Boxed
residues are highly conserved amongst HPt domains. Light gray
shading indicates hydrophobic residues that have a periodicity
(i, i + 3, i + 4) consistent with amphipathic antiparallel
helices as in YPD1. Dark gray shading highlights residues that
are size-conserved. Residues shaded in blue are positively
charged side-chains near the active-site histidine residue that
may be important for stabilizing the phospho-histidine and/or
stabilizing the transition state during phosphoryl transfer.
Residues at position -9, highlighted in pink, have side-chains
that can serve as hydrogen bond acceptors in forming a helix
N-cap. Spo0B, a well-characterized HPt domain from B. subtilis,
does not fit the alignment well due to its dimeric configuration
and an inverted sequence motif with respect to other HPt domains
[Tzeng et al 1998]. Abbreviations: ECOLI, Escherichia coli;
DICTO, Dictyostelium discoideum; RHOSP, Rhodobacter sphaeroides;
PROMI, Proteus mirabilis; MYXXA, Myxococcus xanthus; PSESY,
Pseudomonas syringae; BORBR, Bordetella bronchiseptica; FREDI,
Fremyella diplosiphon; ERWCA, Erwinia carotovora; VIBHA,Vibrio
harveyi; ARATH, Arabidopsis thaliana; BACSU, Bacillus subtilis.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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