7OG7

Crystal structure of the copper chaperone NosL from Shewanella denitrificans

7OG7 の概要

• エントリーDOI: 10.2210/pdb7og7/pdb
• 分子名称: NosL, COPPER (I) ION, ZINC ION, ... (5 entities in total)
• 機能のキーワード: copper chaperone, metal binding protein
• 由来する生物種: Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20654.30

構造登録者

Prasser, B.,Schoener, L.,Zhang, L.,Einsle, O. (登録日: 2021-05-06, 公開日: 2021-07-07, 最終更新日: 2024-06-19)

主引用文献

Prasser, B.,Schoner, L.,Zhang, L.,Einsle, O.
The Copper Chaperone NosL Forms a Heterometal Site for Cu Delivery to Nitrous Oxide Reductase.
Angew.Chem.Int.Ed.Engl., 60:18810-18814, 2021

PubMed Abstract: The final step of denitrification is the reduction of nitrous oxide (N O) to N , mediated by Cu-dependent nitrous oxide reductase (N OR). Its metal centers, Cu and Cu , are assembled through sequential provision of twelve Cu ions by a metallochaperone that forms part of a nos gene cluster encoding the enzyme and its accessory factors. The chaperone is the nosL gene product, an 18 kDa lipoprotein predicted to reside in the outer membrane of Gram-negative bacteria. In order to better understand the assembly of N OR, we have produced NosL from Shewanella denitrificans and determined the structure of the metal-loaded chaperone by X-ray crystallography. The protein assembled a heterodinuclear metal site consisting of Zn and Cu , as evidenced by anomalous X-ray scattering. While only Cu is delivered to the enzyme, the stabilizing presence of Zn is essential for the functionality and structural integrity of the chaperone.

PubMed: 34171184
DOI: 10.1002/anie.202106348

実験手法

X-RAY DIFFRACTION (1.85 Å)