8PBW

Histidine-containing phosphotransfer protein from Chaetomium thermophilum

8PBW の概要

• エントリーDOI: 10.2210/pdb8pbw/pdb
• 分子名称: HPt domain-containing protein, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: histidine-containing phosphotransferase, fungal, phosphorelay, transferase
• 由来する生物種: Thermochaetoides thermophila
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 75877.18

構造登録者

Paredes-Martinez, F.,Casino, P. (登録日: 2023-06-09, 公開日: 2024-07-03, 最終更新日: 2024-07-17)

主引用文献

Paredes-Martinez, F.,Eixeres, L.,Zamora-Caballero, S.,Casino, P.
Structural and functional insights underlying recognition of histidine phosphotransfer protein in fungal phosphorelay systems.
Commun Biol, 7:814-814, 2024

PubMed Abstract: In human pathogenic fungi, receiver domains from hybrid histidine kinases (hHK) have to recognize one HPt. To understand the recognition mechanism, we have assessed phosphorelay from receiver domains of five hHKs of group III, IV, V, VI, and XI to HPt from Chaetomium thermophilum and obtained the structures of Ct_HPt alone and in complex with the receiver domain of hHK group VI. Our data indicate that receiver domains phosphotransfer to Ct_HPt, show a low affinity for complex formation, and prevent a Leu-Thr switch to stabilize phosphoryl groups, also derived from the structures of the receiver domains of hHK group III and Candida albicans Sln1. Moreover, we have elucidated the envelope structure of C. albicans Ypd1 using small-angle X-ray scattering which reveals an extended flexible conformation of the long loop αD-αE which is not involved in phosphotransfer. Finally, we have analyzed the role of salt bridges in the structure of Ct_HPt alone.

PubMed: 38965424
DOI: 10.1038/s42003-024-06459-0

実験手法

X-RAY DIFFRACTION (2.4 Å)