8GBK
Dri1 hemoprotein variant H79A-R90A with a zinc-mirror heme site
Summary for 8GBK
Entry DOI | 10.2210/pdb8gbk/pdb |
Related | 8FM6 |
Descriptor | Ssr1698 protein, HEME B/C (2 entities in total) |
Functional Keywords | metal binding protein, heme, dri domain |
Biological source | Synechocystis sp. PCC 6803 substr. Kazusa |
Total number of polymer chains | 8 |
Total formula weight | 91702.25 |
Authors | |
Primary citation | 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 Cited by 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: 38609367DOI: 10.1038/s41467-024-47486-z PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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