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PDBsum entry 1wn0
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Signaling protein
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PDB id
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1wn0
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Contents |
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131 a.a.
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124 a.a.
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138 a.a.
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References listed in PDB file
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Key reference
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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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Abstract
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In higher plants, histidine-aspartate phosphorelays (two-component system) are
involved in hormone signaling and stress responses. In these systems,
histidine-containing phosphotransfer (HPt) proteins mediate the signal
transmission from sensory histidine kinases to response regulators, including
integration of several signaling pathways or branching into different pathways.
We have determined the crystal structure of a maize HPt protein, ZmHP2, at 2.2 A
resolution. ZmHP2 has six alpha-helices with a four-helix bundle at the
C-terminus, a feature commonly found in HPt domains. In ZmHP2, almost all of the
conserved residues among plant HPt proteins surround this histidine, probably
forming the docking interface for the receiver domain of histidine kinase or the
response regulator. Arg102 of ZmHP2 is conserved as a basic residue in plant HPt
proteins. In bacteria, it is replaced by glutamine or glutamate that form a
hydrogen bond to Ndelta atoms of the phospho-accepting histidine. It may play a
key role in the complex formation of ZmHP2 with receiver domains.
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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
reprinted
by permission from the Protein Society:
Protein Sci
(2005,
14,
202-208)
copyright 2005.
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