6l1h

Crystal structure of light-dependent protochlorophyllide oxidoreductase from Thermosynechococcus elongatus

spinqualitylabelsall models 6l1h, resolution 2.41Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6l1h is a 2 chain structure with sequence from Thermosynechococcus vestitus BP-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.409Å Ligands: NDP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8DLC1_THEVB Phototransformation of protochlorophyllide (Pchlide) to chlorophyllide (Chlide).[RuleBase:RU365001] Publication Abstract from PubMed 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 structure-function relationships of the light-driven Pchlide reduction. Crystal structures of cyanobacterial light-dependent protochlorophyllide oxidoreductase.,Dong CS, Zhang WL, Wang Q, Li YS, Wang X, Zhang M, Liu L Proc Natl Acad Sci U S A. 2020 Mar 31. pii: 1920244117. doi:, 10.1073/pnas.1920244117. PMID:32234783 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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