7VOS

High-resolution neutron and X-ray joint refined structure of high-potential iron-sulfur protein in the oxidized state

7VOS の概要

• エントリーDOI: 10.2210/pdb7vos/pdb
• 分子名称: High-potential iron-sulfur protein, IRON/SULFUR CLUSTER, SULFATE ION, ... (7 entities in total)
• 機能のキーワード: iron-sulfur protein, metal binding protein
• 由来する生物種: Thermochromatium tepidum (Chromatium tepidum)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10180.47

構造登録者

Hanazono, Y.,Hirano, Y.,Takeda, K.,Kusaka, K.,Tamada, T.,Miki, K. (登録日: 2021-10-14, 公開日: 2022-06-01, 最終更新日: 2024-04-03)

主引用文献

Hanazono, Y.,Hirano, Y.,Takeda, K.,Kusaka, K.,Tamada, T.,Miki, K.
Revisiting the concept of peptide bond planarity in an iron-sulfur protein by neutron structure analysis.
Sci Adv, 8:eabn2276-eabn2276, 2022

PubMed Abstract: The planarity of the peptide bond is important for the stability and structure formation of proteins. However, substantial distortion of peptide bonds has been reported in several high-resolution structures and computational analyses. To investigate the peptide bond planarity, including hydrogen atoms, we report a 1.2-Å resolution neutron structure of the oxidized form of high-potential iron-sulfur protein. This high-resolution neutron structure shows that the nucleus positions of the amide protons deviate from the peptide plane and shift toward the acceptors. The planarity of the H─N─C═O plane depends strongly on the pyramidalization of the nitrogen atom. Moreover, the orientation of the amide proton of Cys is different in the reduced and oxidized states, possibly because of the electron storage capacity of the iron-sulfur cluster.

PubMed: 35594350
DOI: 10.1126/sciadv.abn2276

実験手法

NEUTRON DIFFRACTION (1.2 Å)
X-RAY DIFFRACTION (0.66 Å)