PMID:10089421
| Citation |
Hamada, K, Kato, M, Mizuno, T and Hakoshima, T (1999) Crystallographic characterization of a novel protein SixA which exhibits phospho-histidine phosphatase activity in the multistep His-Asp phosphorelay. Acta Crystallogr. D Biol. Crystallogr. 55:269-71 |
|---|---|
| Abstract |
SixA has been isolated from Escherichia coli as the first protein to exhibit phospho-histidine phosphatase activity. Recent biochemical studies have shown that SixA is involved in the signal transduction of the His-Asp phosphorelay through the dephosphorylation of the histidine-containing phosphotransfer (HPt) domain of the anaerobic sensor kinase ArcB. Crystals of SixA were obtained using a hanging-drop vapour-diffusion method with polyethylene glycol and calcium ions. Preliminary X-ray crystallographic analysis revealed that the crystals belonged to space group P212121 with unit-cell dimensions a = 39.26, b = 48.62 and c = 83.18 A, having one molecule in the crystallographic asymmetric unit. The intensity data were collected up to 1.5 A resolution using synchrotron radiation. |
| Links |
PubMed Online version:10.1107/S0907444998007756 |
| Keywords |
Aspartic Acid/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/isolation & purification; Bacterial Proteins/metabolism; Crystallization; Crystallography, X-Ray; Escherichia coli/chemistry; Escherichia coli/metabolism; Escherichia coli Proteins; Histidine/metabolism; Membrane Proteins/metabolism; Phosphoric Monoester Hydrolases/chemistry; Phosphoric Monoester Hydrolases/isolation & purification; Phosphoric Monoester Hydrolases/metabolism; Protein Kinases; Signal Transduction |
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