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PDBsum entry 1or6
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Signaling protein
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PDB id
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1or6
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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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Structure of the oxygen sensor in bacillus subtilis: signal transduction of chemotaxis by control of symmetry.
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Authors
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W.Zhang,
G.N.Phillips.
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Ref.
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Structure, 2003,
11,
1097-1110.
[DOI no: ]
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PubMed id
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Abstract
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Much is now known about chemotaxis signaling transduction for Escherichia coli
and Salmonella typhimurium. The mechanism of chemotaxis of Bacillus subtilis is,
in a sense, reversed. Attractant binding strengthens the activity of histidine
kinase in B. subtilis, instead of an inhibition reaction. The HemAT from B.
subtilis can detect oxygen and transmit the signal to regulatory proteins that
control the direction of flagella rotation. We have determined the crystal
structures of the HemAT sensor domain in liganded and unliganded forms at 2.15 A
and 2.7 A resolution, respectively. The liganded structure reveals a highly
symmetrical organization. Tyrosine70 shows distinct conformational changes on
one subunit when ligands are removed. Our study suggests that disruption of the
symmetry of HemAT plays an important role in initiating the chemotaxis signaling
transduction cascade.
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Figure 1.
Figure 1. The Molecular Structure of the HemAT Sensor
Domain Represented with Ribbon Diagrams(A) Stereo view of the
structure. The signaling domain would be located further down on
the page.(B) Top view showing the flanking of the core helices,
G and H, by the rest of the molecule. The helices are labeled
corresponding to the nomenclature of the globin fold. Subunit A,
cyan; subunit B, yellow.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2003,
11,
1097-1110)
copyright 2003.
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