6L1G

Crystal structure of light-dependent protochlorophyllide oxidoreductase from Synechocystis sp. PCC 6803

Summary for 6L1G

• Entry DOI: 10.2210/pdb6l1g/pdb
• Descriptor: Light-dependent protochlorophyllide reductase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, SULFATE ION, ... (4 entities in total)
• Functional Keywords: chlorophyll biosynthesis, photocatalysis, nadph, oxidoreductase
• Biological source: Synechocystis sp. (strain PCC 6803 / Kazusa)
• Total number of polymer chains: 2
• Total formula weight: 78436.95

Authors

Dong, C.,Wang, X.,Liu, L. (deposition date: 2019-09-29, release date: 2020-04-01, Last modification date: 2023-11-22)

Primary citation

Dong, C.S.,Zhang, W.L.,Wang, Q.,Li, Y.S.,Wang, X.,Zhang, M.,Liu, L.
Crystal structures of cyanobacterial light-dependent protochlorophyllide oxidoreductase.
Proc.Natl.Acad.Sci.USA, 117:8455-8461, 2020

PubMed Abstract: 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, sp. and 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 structure-function relationships of the light-driven Pchlide reduction.

PubMed: 32234783
DOI: 10.1073/pnas.1920244117

Experimental method

X-RAY DIFFRACTION (2.2 Å)