7DMO

Crystal structures of two pericyclases catalyzing [4+2] cycloadditions

Summary for 7DMO

• Entry DOI: 10.2210/pdb7dmo/pdb
• Descriptor: Diels-Alderase (2 entities in total)
• Functional Keywords: [4+2]-pericyclase, biosynthetic protein, isomerase
• Biological source: Pyrenochaetopsis sp.
• Total number of polymer chains: 6
• Total formula weight: 250512.33

Authors

Wang, Z.D.,Chi, C.B.,Ma, M. (deposition date: 2020-12-04, release date: 2021-10-06, Last modification date: 2023-11-29)

Primary citation

Chi, C.,Wang, Z.,Liu, T.,Zhang, Z.,Zhou, H.,Li, A.,Jin, H.,Jia, H.,Yin, F.,Yang, D.,Ma, M.
Crystal Structures of Fsa2 and Phm7 Catalyzing [4 + 2] Cycloaddition Reactions with Reverse Stereoselectivities in Equisetin and Phomasetin Biosynthesis.
Acs Omega, 6:12913-12922, 2021

PubMed Abstract: Fsa2 and Phm7 are a unique pair of pericyclases catalyzing [4 + 2] cycloaddition reactions with reverse stereoselectivities in the biosynthesis of equisetin and phomasetin, both of which are potent HIV-1 integrase inhibitors. We here solve the crystal structures of Fsa2 and Phm7, both of which possess unusual "two-β barrel" folds. Different residues are evident between the active sites of Fsa2 and Phm7, and modeling experiments provide key structural information determining the reverse stereoselectivities. These results provide a better understanding of how natural pericyclases control the catalytic stereoselectivities and benefit the protein engineering in future.

PubMed: 34056443
DOI: 10.1021/acsomega.1c01593

Experimental method

X-RAY DIFFRACTION (2 Å)