Crystal structures of cyanobacterial light-dependent protochlorophyllide oxidoreductase

The reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) is the penultimate step of chlorophyll biosynthesis. In oxygenic photosynthetic bacteria, algae, and plants, this reaction can be catalyzed by the light-dependent Pchlide oxidoreductase (LPOR), a member of the short-chain dehy...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2020-04, Vol.117 (15), p.8455-8461
Main Authors: Dong, Chen-Song, Zhang, Wei-Lun, Wang, Qiao, Li, Yu-Shuai, Wang, Xiao, Zhang, Min, Liu, Lin
Format: Article
Language:English
Subjects:
Algae
Biological Sciences
Biosynthesis
Catalytic activity
Chlorophyll
Computer simulation
Crystal structure
Cyanobacteria
Elongated structure
NAD
NADP
Oxidoreductase
Photosynthesis
Protochlorophyllide
Reduction
Structural analysis
Structure-function relationships
Substrates
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Summary:The reduction of protochlorophyllide (Pchlide) to chlorophyllide (Chlide) is the penultimate step of chlorophyll biosynthesis. In oxygenic photosynthetic bacteria, algae, and plants, this reaction can be catalyzed by the light-dependent Pchlide oxidoreductase (LPOR), a member of the short-chain dehydrogenase superfamily sharing a conserved Rossmann fold for NAD(P)H binding and the catalytic activity. Whereas modeling and simulation approaches have been used to study the catalytic mechanism of this light-driven reaction, key details of the LPOR structure remain unclear. We determined the crystal structures of LPOR from two cyanobacteria, Synechocystis sp. PCC 6803 and Thermosynechococcus elongatus. Structural analysis defines the LPOR core fold, outlines the LPOR–NADPH interaction network, identifies the residues forming the substrate cavity and the proton-relay path, and reveals the role of the LPOR-specific loop. These findings provide a basis for understanding the structurefunction relationships of the light-driven Pchlide reduction.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1920244117