6JZS

Structure of the Manganese Protoporphyrin IX-Reconstituted CYP102A1 Haem Domain with N-Abietoyl-L-Tryptophan in complex with Pyridine

Summary for 6JZS

• Entry DOI: 10.2210/pdb6jzs/pdb
• Descriptor: Bifunctional cytochrome P450/NADPH--P450 reductase, pyridine, (2S)-2-[[(1R,4aR,4bR,10aR)-1,4a-dimethyl-7-propan-2-yl-2,3,4,4b,5,6,10,10a-octahydrophenanthren-1-yl]carbonylamino]-3-( 1H-indol-3-yl)propanoic acid, ... (6 entities in total)
• Functional Keywords: monooxygenase, oxidoreductase
• Biological source: Bacillus megaterium
• Total number of polymer chains: 2
• Total formula weight: 115322.05

Authors

Stanfield, J.K.,Omura, K.,Matsumoto, A.,Kasai, C.,Sugimoto, H.,Shiro, Y.,Watanabe, Y.,Shoji, O. (deposition date: 2019-05-03, release date: 2020-03-18, Last modification date: 2023-11-22)

Primary citation

Stanfield, J.K.,Omura, K.,Matsumoto, A.,Kasai, C.,Sugimoto, H.,Shiro, Y.,Watanabe, Y.,Shoji, O.
Crystals in Minutes: Instant On-Site Microcrystallisation of Various Flavours of the CYP102A1 (P450BM3) Haem Domain.
Angew.Chem.Int.Ed.Engl., 59:7611-7618, 2020

PubMed Abstract: Despite CYP102A1 (P450BM3) representing one of the most extensively researched metalloenzymes, crystallisation of its haem domain upon modification can be a challenge. Crystal structures are indispensable for the efficient structure-based design of P450BM3 as a biocatalyst. The abietane diterpenoid derivative N-abietoyl-l-tryptophan (AbiATrp) is an outstanding crystallisation accelerator for the wild-type P450BM3 haem domain, with visible crystals forming within 2 hours and diffracting to a near-atomic resolution of 1.22 Å. Using these crystals as seeds in a cross-microseeding approach, an assortment of P450BM3 haem domain crystal structures, containing previously uncrystallisable decoy molecules and diverse artificial metalloporphyrins binding various ligand molecules, as well as heavily tagged haem-domain variants, could be determined. Some of the structures reported herein could be used as models of different stages of the P450BM3 catalytic cycle.

PubMed: 32157795
DOI: 10.1002/anie.201913407

Experimental method

X-RAY DIFFRACTION (1.68 Å)