1or6
From Proteopedia
Crystal Structure of HemAT sensor domain from B.subtilis in the unliganded form
Structural highlights
FunctionHEMAT_BACSU Heme-containing signal transducer responsible for aerotaxis, the migratory response toward or away from oxygen.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMuch 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. Structure of the oxygen sensor in Bacillus subtilis: signal transduction of chemotaxis by control of symmetry.,Zhang W, Phillips GN Jr Structure. 2003 Sep;11(9):1097-110. PMID:12962628[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
