6JJS

Crystal structure of an enzyme from Penicillium herquei in condition2

Summary for 6JJS

• Entry DOI: 10.2210/pdb6jjs/pdb
• Descriptor: PhnH, ACETATE ION (3 entities in total)
• Functional Keywords: prenyltransferase, transferase
• Biological source: Penicillium herquei
• Total number of polymer chains: 1
• Total formula weight: 16282.08

Authors

Fen, Y.,Huang, J.W.,Liu, W.D.,Chen, C.C.,Guo, R.T. (deposition date: 2019-02-26, release date: 2020-01-01, Last modification date: 2023-11-22)

Primary citation

Feng, Y.,Yu, X.,Huang, J.W.,Liu, W.,Li, Q.,Hu, Y.,Yang, Y.,Chen, Y.,Jin, J.,Li, H.,Chen, C.C.,Guo, R.T.
Crystal structure and proposed mechanism of an enantioselective hydroalkoxylation enzyme from Penicillium herquei.
Biochem.Biophys.Res.Commun., 516:801-805, 2019

PubMed Abstract: Hydroalkoxylation is a useful and efficient reaction which generates C-O bond and produces cyclic ethers, the common structural elements of natural products. The dedicative enzyme which can catalyze enantioselective hydroalkoxylation named PhnH was recently identified in the herqueinone biosynthetic gene from Penicillium herquei. It catalyzes addition of a phenol to the terminal olefin on substrate to produce a dihydrobenzofuran. Here, the crystal structure of PhnH is reported and the putative substrate-binding pocket is illustrated. Through docking experiment, possible substrate-binding poses are displayed and the catalytic mechanism is therefore proposed. Our findings form the basis for further studies of enantioselective hydroalkoxylation enzymes.

PubMed: 31256936
DOI: 10.1016/j.bbrc.2019.06.100

Experimental method

X-RAY DIFFRACTION (1.62 Å)