7x8k
From Proteopedia
Arabidopsis GDP-D-mannose pyrophosphorylase (VTC1) structure (product-bound)
Structural highlights
FunctionGMPP1_ARATH Essential protein during embryogenesis (PubMed:15266054). Catalyzes a reaction of the Smirnoff-Wheeler pathway, the major route to ascorbate biosynthesis in plants. Plays an essential role in plant growth and development and cell-wall architecture. Provides GDP-mannose, used for cell wall carbohydrate biosynthesis, protein N-glycosylation, as well as for the biosynthesis of the antioxidant ascorbate.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11] [12] Publication Abstract from PubMedPlant GDP-D-mannose pyrophosphorylase (GMPase) catalyzes a committed step in ascorbic acid biosynthesis pathway. Arabidopsis thaliana VTC1 is the first genetically characterized plant GMPase and has unique properties when compared with bacterial and animal homologs. Here we present the crystal structures of VTC1 in the unliganded and product-bound states at resolutions of 2.8 and 3.0 A, respectively. VTC1 dimerizes in a same way like other known GMPases, but dodecamerizes in a previously unobserved arrangement. The interactions to GDP-D-mannose and inorganic pyrophosphate are revealed by the product-bound VTC1 structure. An in vitro GMPase activity assay confirms the regulatory role of the C-terminal left-handed beta-helix domain, and structural analyses suggest the models of VTC1 hetero-complex with its interacting proteins. The structural information advances our insights into the different mechanisms involved in VTC1 regulation. Crystal Structures of Arabidopsis thaliana GDP-D-Mannose Pyrophosphorylase VITAMIN C DEFECTIVE 1.,Zhang C, Zhao S, Li YS, He C, Wang X, Liu L Front Plant Sci. 2022 May 23;13:899738. doi: 10.3389/fpls.2022.899738., eCollection 2022. PMID:35677252[13] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found References
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