6K2H

structural characterization of mutated NreA protein in nitrate binding site from staphylococcus aureus.

6K2H の概要

• エントリーDOI: 10.2210/pdb6k2h/pdb
• 分子名称: NreA, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: complex, signaling protein
• 由来する生物種: Staphylococcus aureus subsp. aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17268.95

構造登録者

Sangare, L.,Chen, W.,Wang, C.,Chen, X.,Wu, M.,Zhang, X.,Zang, J. (登録日: 2019-05-14, 公開日: 2020-03-11, 最終更新日: 2023-11-22)

主引用文献

Sangare, L.,Chen, W.,Wang, C.,Chen, X.,Wu, M.,Zhang, X.,Zang, J.
Structural insights into the conformational change of Staphylococcus aureus NreA at C-terminus.
Biotechnol.Lett., 42:787-795, 2020

PubMed Abstract: Staphylococcus aureus is an anaerobic facultative microorganism that features the NreABC system for nitrate respiration. NreB is the sensor histidine kinase that phosphorylates the response regulator NreC to stimulate the expression of target genes. NreA is a nitrate sensor which dissociates from NreB in the present of nitrate and relieves its inhibition on NreB. However, the molecular basis of how NreA regulate NreB remains unknown. In this study, we determined the crystal structures of nitrate-bound NreA from S. aureus (SaNreA/NO) and its apoNreA-like mutant SaNreAY in complex with ethanediol (SaNreA/EDO). Structural comparison reveals that the C-terminal loop in SaNreA/NO rearranges to an α-helix (α7) in SaNreA/EDO, which converts an acidic pocket on the surface to a positively charged region. This conformational change of SaNreA C-terminus might play a role in SaNreB binding.

PubMed: 31970556
DOI: 10.1007/s10529-020-02807-2

実験手法

X-RAY DIFFRACTION (1.8 Å)