7EQH

Crystal structure of Arabidopsis GUN2/HO1 in complex with heme

Summary for 7EQH

• Entry DOI: 10.2210/pdb7eqh/pdb
• Descriptor: Heme oxygenase 1, chloroplastic, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: arabidopsis, gun2, heme oxygenase, heme metabolism, heme, biliverdin, oxidoreductase
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Total number of polymer chains: 2
• Total formula weight: 56709.61

Authors

Li, X.,Wang, J.,Liu, L. (deposition date: 2021-05-02, release date: 2022-05-11, Last modification date: 2023-11-29)

Primary citation

Wang, J.,Li, X.,Chang, J.W.,Ye, T.,Mao, Y.,Wang, X.,Liu, L.
Enzymological and structural characterization of Arabidopsis thaliana heme oxygenase-1.
Febs Open Bio, 12:1677-1687, 2022

PubMed Abstract: Arabidopsis thaliana heme oxygenase-1 (AtHO-1), a metabolic enzyme in the heme degradation pathway, serves as a prototype for study of the bilin-related functions in plants. Past biological analyses revealed that AtHO-1 requires ferredoxin-NADP reductase (FNR) and ferredoxin for its enzymatic activity. Here, we characterized the binding and degradation of heme by AtHO-1, and found that ferredoxin is a dispensable component of the reducing system that provides electrons for heme oxidation. Furthermore, we reported the crystal structure of heme-bound AtHO-1, which demonstrates both conserved and previously undescribed features of plant heme oxygenases. Finally, the electron transfer pathway from FNR to AtHO-1 is suggested based on the known structural information.

PubMed: 35689519
DOI: 10.1002/2211-5463.13453

Experimental method

X-RAY DIFFRACTION (2.2 Å)