8ZXQ

Crystal structure of Ssr1698 in complex with heme b

Summary for 8ZXQ

• Entry DOI: 10.2210/pdb8zxq/pdb
• Descriptor: Ssr1698 protein, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: ssr1698, heme b, heme c, metal binding protein
• Biological source: Synechocystis sp. (strain PCC 6803 / Kazusa)
• Total number of polymer chains: 1
• Total formula weight: 12259.62

Authors

Wang, X.,Liu, L. (deposition date: 2024-06-14, release date: 2024-12-25, Last modification date: 2025-04-16)

Primary citation

Wang, X.Y.,Zhang, J.,Li, H.Y.,Dong, C.S.,Dai, H.E.,Wang, M.,Liu, L.
Structural Basis for Monomer-Dimer Transition of Dri1 Upon Heme Binding.
Proteins, 93:949-956, 2025

PubMed Abstract: Domain related to iron (DRI) contains approximately 90 residues and is involved in iron and heme metabolism. Recent discoveries have annotated Dri1, a DRI-only protein from the cyanobacterium Synechocystis, as a regulator of succinate dehydrogenase in a b-type heme-dependent manner or as a c-type heme oxygenase. Here, we report high-resolution structures of Dri1 in complex with b-type and c-type hemes, respectively. Bis-His-ligated heme is located in the middle of the dimeric Dri1 complex with heme b, as well as in the complex of monomeric Dri1 with c-type heme, but distinct heme binding modes are revealed. Structural analyses suggest that Dri1 may participate in the succinate dehydrogenase activity and/or the metabolism of cytochromes.

PubMed: 39670557
DOI: 10.1002/prot.26778

Experimental method

X-RAY DIFFRACTION (1.51 Å)