1FR0

SOLUTION STRUCTURE OF THE HISTIDINE-CONTAINING PHOSPHOTRANSFER DOMAIN OF ANAEROBIC SENSOR KINASE ARCB FROM ESCHERICHIA COLI.

1FR0 の概要

• エントリーDOI: 10.2210/pdb1fr0/pdb
• 関連するPDBエントリー: 2a0b
• 分子名称: ARCB (1 entity in total)
• 機能のキーワード: four-helix bundle motif, anaerobic sensor kinase, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P22763
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14013.94

構造登録者

Ikegami, T.,Okada, T.,Ohki, I.,Hirayama, J.,Mizuno, T.,Shirakawa, M. (登録日: 2000-09-07, 公開日: 2001-03-14, 最終更新日: 2024-05-29)

主引用文献

Ikegami, T.,Okada, T.,Ohki, I.,Hirayama, J.,Mizuno, T.,Shirakawa, M.
Solution structure and dynamic character of the histidine-containing phosphotransfer domain of anaerobic sensor kinase ArcB from Escherichia coli.
Biochemistry, 40:375-386, 2001

PubMed Abstract: An Escherichia coli sensor kinase, ArcB, transfers a phosphoryl group to a partner response regulator in response to anaerobic conditions. Multidimensional NMR techniques were applied to determine the solution structure of the histidine-containing phosphotransfer signaling domain of ArcB (HPt(ArcB)), which has a phosphorylation site, His717. The backbone dynamics were also investigated by analyses of the (15)N relaxation data and amide hydrogen exchange rates. Furthermore, the protonation states of the histidine imidazole rings were characterized by means of (1)H and (15)N chemical shifts at various pHs. The determined solution structure of HPt(ArcB) contains five helices and forms a four-helix bundle motif like other HPt domains. The obtained order parameters, S (2), [(1)H]-(15)N heteronuclear NOE values, and chemical exchange parameters, R(ex), showed that the alpha-helical regions of HPt(ArcB) are rigid on both picosecond to nanosecond and microsecond to millisecond time scales. On the other hand, helix D, which contains His717, exhibited low protection factors of less than 4000, indicating the presence of fluctuations on a slower time scale in helix D. These results suggest that HPt(ArcB) may undergo a small conformational change in helix D upon phosphorylation. It was also shown that the imidazole ring of His717 has a pK(a) value of 6.76, which is similar to that of a solvent-exposed histidine imidazole ring, and that a pair of deprotonated neutral tautomers are rapidly exchanged with each other. This is consistent with the solution structure of HPt(ArcB), in which the imidazole ring of His717 is exposed to the solvent.

PubMed: 11148031
DOI: 10.1021/bi001619g

実験手法

SOLUTION NMR