7Q4G

Structure of coproheme decarboxylase from Corynebacterium dipththeriae Y135A mutant in complex with coproheme

Summary for 7Q4G

• Entry DOI: 10.2210/pdb7q4g/pdb
• Descriptor: Coproheme decarboxylase from Corynebacterium diphtheriae Y135A mutant in complex with coproheme, 1,3,5,8-TETRAMETHYL-PORPHINE-2,4,6,7-TETRAPROPIONIC ACID FERROUS COMPLEX, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: coproheme decarboxylase, coproporphyrin dependent heme b biosynthesis, porphyrin binding alpha-beta barrel protein, biosynthetic protein
• Biological source: Corynebacterium diphtheriae
• Total number of polymer chains: 5
• Total formula weight: 139633.14

Authors

Michlits, H.,Valente, N.,Mlynek, G.,Hofbauer, S. (deposition date: 2021-10-30, release date: 2022-02-23, Last modification date: 2024-01-31)

Primary citation

Michlits, H.,Valente, N.,Mlynek, G.,Hofbauer, S.
Initial Steps to Engineer Coproheme Decarboxylase to Obtain Stereospecific Monovinyl, Monopropionyl Deuterohemes.
Front Bioeng Biotechnol, 9:807678-807678, 2021

PubMed Abstract: The oxidative decarboxylation of coproheme to form heme by coproheme decarboxylase is a stereospecific two-step reaction. In the first step, the propionate at position two (p2) is cleaved off the pyrrole ring A to form a vinyl group at this position. Subsequently, the propionate at position four (p4) on pyrrole ring B is cleaved off and heme is formed. In this study, we attempted to engineer coproheme decarboxylase from to alter the stereospecificity of this reaction. By introducing a tyrosine residue in proximity to the propionate at position 4, we were able to create a new radical center in the active site. However, the artificial Tyr183 radical could not be shown to catalyze any decarboxylation.

PubMed: 35141216
DOI: 10.3389/fbioe.2021.807678

Experimental method

X-RAY DIFFRACTION (1.82 Å)