3ZRV

The high resolution structure of a dimeric Hamp-Dhp fusion displays asymmetry - A291F mutant

3ZRV の概要

• エントリーDOI: 10.2210/pdb3zrv/pdb
• 関連するPDBエントリー: 1BXD 1JOY 1NJV 2Y0Q 2Y0T 2Y20 2Y21 3ZRW 3ZRX
• 分子名称: HAMP, OSMOLARITY SENSOR PROTEIN ENVZ (2 entities in total)
• 機能のキーワード: signaling protein, signalling protein, hamp, signalling
• 由来する生物種: ARCHAEOGLOBUS FULGIDUS; 詳細
• 細胞内の位置: Cell inner membrane; Multi-pass membrane protein: P0AEJ4
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 26369.89

構造登録者

Zeth, K.,Hulko, M.,Ferris, H.U.,Martin, J. (登録日: 2011-06-20, 公開日: 2011-07-06, 最終更新日: 2024-05-08)

主引用文献

Ferris, H.U.,Dunin-Horkawicz, S.,Hornig, N.,Hulko, M.,Martin, J.,Schultz, J.E.,Zeth, K.,Lupas, A.N.,Coles, M.
Mechanism of Regulation of Receptor Histidine Kinases.
Structure, 20:56-, 2012

PubMed Abstract: Bacterial transmembrane receptors regulate an intracellular catalytic output in response to extracellular sensory input. To investigate the conformational changes that relay the regulatory signal, we have studied the HAMP domain, a ubiquitous intracellular module connecting input to output domains. HAMP forms a parallel, dimeric, four-helical coiled coil, and rational substitutions in our model domain (Af1503 HAMP) induce a transition in its interhelical packing, characterized by axial rotation of all four helices (the gearbox signaling model). We now illustrate how these conformational changes are propagated to a downstream domain by fusing Af1503 HAMP variants to the DHp domain of EnvZ, a bacterial histidine kinase. Structures of wild-type and mutant constructs are correlated with ligand response in vivo, clearly associating them with distinct signaling states. We propose that altered recognition of the catalytic domain by DHp, rather than a shift in position of the phospho-accepting histidine, forms the basis for regulation of kinase activity.

PubMed: 22244755
DOI: 10.1016/J.STR.2011.11.014

実験手法

X-RAY DIFFRACTION (1.65 Å)