6L1G

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

6L1G の概要

• エントリーDOI: 10.2210/pdb6l1g/pdb
• 分子名称: Light-dependent protochlorophyllide reductase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: chlorophyll biosynthesis, photocatalysis, nadph, oxidoreductase
• 由来する生物種: Synechocystis sp. (strain PCC 6803 / Kazusa)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 78436.95

構造登録者

Dong, C.,Wang, X.,Liu, L. (登録日: 2019-09-29, 公開日: 2020-04-01, 最終更新日: 2023-11-22)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)