Structural highlights
Function
[ARCB_ECOLI] Member of the two-component regulatory system ArcB/ArcA. Sensor-regulator protein for anaerobic repression of the arc modulon. Activates ArcA via a four-step phosphorelay. ArcB can also dephosphorylate ArcA by a reverse phosphorelay involving His-717 and Asp-576.
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 PubMed
The crystal structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli has been refined to 1.57 A resolution, using the coordinates of the earlier 2.06 A structure as a starting model. The final model contained 956 protein atoms, one zinc ion and 156 water molecules, with an R factor of 19.0%. The high-resolution electron-density maps clearly revealed additional solvent molecules and seven discrete rotamers in the protein side chains. One residue, Met755, was fully buried but was able to occupy the space in the hydrophobic core by means of the two-state conformation of its side chain. One water molecule was buried in the protein core and contributed to the rigidity of the HPt domain, cooperating in the coordination of the zinc ion.
Refined structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli at 1.57 A resolution.,Kato M, Mizuno T, Shimizu T, Hakoshima T Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1842-9. PMID:10531481[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kato M, Mizuno T, Shimizu T, Hakoshima T. Refined structure of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB from Escherichia coli at 1.57 A resolution. Acta Crystallogr D Biol Crystallogr. 1999 Nov;55(Pt 11):1842-9. PMID:10531481
