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1OR6

Crystal Structure of HemAT sensor domain from B.subtilis in the unliganded form

Summary for 1OR6
Entry DOI10.2210/pdb1or6/pdb
Related1OR4
DescriptorHeme-based aerotactic transducer hemAT, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
Functional Keywordsglobin fold, signaling protein
Biological sourceBacillus subtilis
Total number of polymer chains2
Total formula weight42915.16
Authors
Zhang, W.,Phillips Jr., G.N. (deposition date: 2003-03-11, release date: 2003-09-23, Last modification date: 2023-08-16)
Primary citationZhang, W.,Phillips, G.N.
Structure of the oxygen sensor in Bacillus subtilis: signal transduction of chemotaxis by control of symmetry.
Structure, 11:1097-1110, 2003
Cited by
PubMed Abstract: 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.
PubMed: 12962628
DOI: 10.1016/S0969-2126(03)00169-2
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.71 Å)
Structure validation

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