8FM6

Dri1 hemoprotein variant H21A with a zinc-mirror heme site

8FM6 の概要

• エントリーDOI: 10.2210/pdb8fm6/pdb
• 分子名称: Ssr1698 protein, HEME B/C (2 entities in total)
• 機能のキーワード: metal binding protein, heme, dri domain
• 由来する生物種: Synechocystis sp. PCC 6803
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23097.80

構造登録者

Yee, E.F.,Blaby-Haas, C. (登録日: 2022-12-22, 公開日: 2024-04-24)

主引用文献

Grosjean, N.,Yee, E.F.,Kumaran, D.,Chopra, K.,Abernathy, M.,Biswas, S.,Byrnes, J.,Kreitler, D.F.,Cheng, J.F.,Ghosh, A.,Almo, S.C.,Iwai, M.,Niyogi, K.K.,Pakrasi, H.B.,Sarangi, R.,van Dam, H.,Yang, L.,Blaby, I.K.,Blaby-Haas, C.E.
A hemoprotein with a zinc-mirror heme site ties heme availability to carbon metabolism in cyanobacteria.
Nat Commun, 15:3167-3167, 2024

PubMed Abstract: Heme has a critical role in the chemical framework of the cell as an essential protein cofactor and signaling molecule that controls diverse processes and molecular interactions. Using a phylogenomics-based approach and complementary structural techniques, we identify a family of dimeric hemoproteins comprising a domain of unknown function DUF2470. The heme iron is axially coordinated by two zinc-bound histidine residues, forming a distinct two-fold symmetric zinc-histidine-iron-histidine-zinc site. Together with structure-guided in vitro and in vivo experiments, we further demonstrate the existence of a functional link between heme binding by Dri1 (Domain related to iron 1, formerly ssr1698) and post-translational regulation of succinate dehydrogenase in the cyanobacterium Synechocystis, suggesting an iron-dependent regulatory link between photosynthesis and respiration. Given the ubiquity of proteins containing homologous domains and connections to heme metabolism across eukaryotes and prokaryotes, we propose that DRI (Domain Related to Iron; formerly DUF2470) functions at the molecular level as a heme-dependent regulatory domain.

PubMed: 38609367
DOI: 10.1038/s41467-024-47486-z

実験手法

X-RAY DIFFRACTION (2.85 Å)