2AYY

Solution structure of the E.coli RcsC C-terminus (residues 700-816) containing linker region

2AYY の概要

• エントリーDOI: 10.2210/pdb2ayy/pdb
• 関連するPDBエントリー: 2AYX 2AYZ
• 分子名称: Sensor kinase protein rcsC (1 entity in total)
• 機能のキーワード: new domain, alpha/beta layer, transferase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P14376
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13214.00

構造登録者

Rogov, V.V.,Rogova, N.Y.,Bernhard, F.,Koglin, A.,Lohr, F.,Dotsch, V. (登録日: 2005-09-09, 公開日: 2006-09-26, 最終更新日: 2024-05-29)

主引用文献

Rogov, V.V.,Rogova, N.Y.,Bernhard, F.,Koglin, A.,Lohr, F.,Dotsch, V.
A New Structural Domain in the Escherichia coli RcsC Hybrid Sensor Kinase Connects Histidine Kinase and Phosphoreceiver Domains
J.Mol.Biol., 364:68-79, 2006

PubMed Abstract: The Rcs signalling pathway controls a variety of physiological functions like capsule synthesis, cell division or motility in prokaryotes. The Rcs regulation cascade, involving a multi-step phosphorelay between the two membrane-bound hybrid sensor kinases RcsC and RcsD and the global regulator RcsB, is, up to now, one of the most complicated regulatory systems in bacteria. To understand the structural basis of Rcs signal transduction, NMR spectroscopy was employed to determine the solution structure of the RcsC C terminus, possessing a phosphoreceiver domain (RcsC-PR), and a region previously described as a long linker between the histidine kinase domain of RcsC (RcsC-HK) and the RcsC-PR. We have found that the linker region comprises an independent structural domain of a new alpha/beta organization, which we named RcsC-ABL domain (Alpha/Beta/Loop). The ABL domain appears to be a conserved and unique structural element of RcsC-like kinases with no significant sequence homology to other proteins. The second domain of the C terminus, the RcsC-PR domain, represents a well-folded CheY-like phosphoreceiver domain with the central parallel beta-sheet covered with two alpha-helical layers on both sides. We have mapped the interaction of RcsC-ABL and RcsC-PR with the histidine phosphotransfer domain (HPt) of RcsD. In addition we have characterized the interaction with and the conformational effects of Mg2+ and the phosphorylation mimetic BeF(-)(3) on RcsC-ABL and RcsC-PR.

PubMed: 17005198
DOI: 10.1016/j.jmb.2006.07.052

実験手法

SOLUTION NMR