9JN8

Crystal structure of a thioredoxin-like ferredoxin of Rhodobacter capsulatus

9JN8 の概要

• エントリーDOI: 10.2210/pdb9jn8/pdb
• 分子名称: ORF378, FE2/S2 (INORGANIC) CLUSTER (3 entities in total)
• 機能のキーワード: ferredoxin, [2fe-2s] cluster, thioredoxin fold, electron transport
• 由来する生物種: Rhodobacter capsulatus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 43440.51

構造登録者

Shen, Y.,Liu, L. (登録日: 2024-09-22, 公開日: 2025-02-19, 最終更新日: 2025-04-02)

主引用文献

Shen, Y.H.,Cheng, W.L.,Wang, X.,Dai, H.E.,Wang, M.,Liu, L.
Crystal Structure of a Thioredoxin-like Ferredoxin Encoded Within a Cobalamin Biosynthetic Operon of Rhodobacter capsulatus.
Protein J., 44:192-200, 2025

PubMed Abstract: Thioredoxin-like ferredoxin is a small homodimeric protein containing a [2Fe-2S] cluster in each monomer. It is only found in bacteria but its physiological function remains largely unknown. The cobalamin biosynthetic operon in the genome of the purple phototroph Rhodobacter capsulatus encodes a putative ferredoxin dubbed as CfrX. To characterize this protein, we cloned, expressed, purified, and crystalized the recombinant CfrX in the iron-sulfur cluster-bound state, and solved the structure at 2.1-Å resolution. Adopting a typical thioredoxin-like ferredoxin fold, a CfrX monomer binds one [2Fe-2S] cluster through four Cys residues located on two protruding loops. Unexpectedly, CfrX dimerizes in a previously unreported manner. With the structural information, we ascertained CfrX as a thioredoxin-like ferredoxin. While the precise function of CfrX in cobalamin biosynthesis is elusive, a link between CfrX and aerobic cobaltochelatase should exist due to the gene clustering pattern. We also discussed the possible relationship among CfrX, CobW, and CobNST with respect to the [2Fe-2S] cluster.

PubMed: 39924633
DOI: 10.1007/s10930-025-10254-z

実験手法

X-RAY DIFFRACTION (2.12 Å)