Structural basis for the localization of the chemotaxis phosphatase CheZ by CheAS.
CheA-short interacts with CheZ to localize CheZ to cell poles. The fifth helical region (residues 112 to 133) from the phosphotransfer domain of CheA interacts with CheZ and becomes ordered and helical, although it lacks a stable fold in the CheA fragment comprising residues 98 to 150 alone. One CheA molecule binds to one CheZ dimer.
Hao
Shufeng
S
Department of Chemistry and Biochemistry, University of California-Santa Barbara, Santa Barbara, CA 93106, USA.
Hamel
Damon
D
Zhou
Hongjun
H
Dahlquist
Frederick W
FW
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D002633:Chemotaxis / Q000235:genetics; D019281:Dimerization; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D000071677:Histidine Kinase; D009682:Magnetic Resonance Spectroscopy; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D000072236:Methyl-Accepting Chemotaxis Proteins; D008958:Models, Molecular; D009587:Nitrogen Isotopes; D010766:Phosphorylation; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D011522:Protons; D015398:Signal Transduction
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D000072236:Methyl-Accepting Chemotaxis Proteins; D009587:Nitrogen Isotopes; D011522:Protons; D000071677:Histidine Kinase; C000607608:cheA protein, E coli