6AIQ

High resolution structure of recombinant high-potential iron-sulfur protein

6AIQ の概要

• エントリーDOI: 10.2210/pdb6aiq/pdb
• 分子名称: High-potential iron-sulfur protein, IRON/SULFUR CLUSTER, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: iron-sulfur protein, metal-binding 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: 9906.06

構造登録者

Hanazono, Y.,Takeda, K.,Miki, K. (登録日: 2018-08-24, 公開日: 2019-08-21, 最終更新日: 2023-11-22)

主引用文献

Hanazono, Y.,Takeda, K.,Miki, K.
Characterization of perdeuterated high-potential iron-sulfur protein with high-resolution X-ray crystallography.
Proteins, 88:251-259, 2020

PubMed Abstract: Perdeuteration in neutron crystallography is an effective method for determining the positions of hydrogen atoms in proteins. However, there is shortage of evidence that the high-resolution details of perdeuterated proteins are consistent with those of the nondeuterated proteins. In this study, we determined the X-ray structure of perdeuterated high-potential iron-sulfur protein (HiPIP) at a high resolution of 0.85 å resolution. The comparison of the nondeuterated and perdeuterated structures of HiPIP revealed slight differences between the two structures. The spectroscopic and spectroelectrochemical studies also showed that perdeuterated HiPIP has approximately the same characteristics as nondeuterated HiPIP. These results further emphasize the suitability of using perdeuterated proteins in the high-resolution neutron crystallography.

PubMed: 31365157
DOI: 10.1002/prot.25793

実験手法

X-RAY DIFFRACTION (0.85 Å)