7X8K

Arabidopsis GDP-D-mannose pyrophosphorylase (VTC1) structure (product-bound)

Summary for 7X8K

• Entry DOI: 10.2210/pdb7x8k/pdb
• Descriptor: Mannose-1-phosphate guanylyltransferase 1, GUANOSINE-5'-DIPHOSPHATE-ALPHA-D-MANNOSE, CITRATE ANION, ... (6 entities in total)
• Functional Keywords: ascorbic acid; nucleotide sugar; guanylyltransferase; arabidopsis thaliana, transferase
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 4
• Total formula weight: 168525.27

Authors

Zhao, S.,Zhang, C.,Liu, L. (deposition date: 2022-03-13, release date: 2022-05-18, Last modification date: 2023-11-29)

Primary citation

Zhang, C.,Zhao, S.,Li, Y.S.,He, C.,Wang, X.,Liu, L.
Crystal Structures of Arabidopsis thaliana GDP-D-Mannose Pyrophosphorylase VITAMIN C DEFECTIVE 1.
Front Plant Sci, 13:899738-899738, 2022

PubMed Abstract: Plant GDP-D-mannose pyrophosphorylase (GMPase) catalyzes a committed step in ascorbic acid biosynthesis pathway. 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 Å, 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 GMPase activity assay confirms the regulatory role of the C-terminal left-handed β-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.

PubMed: 35677252
DOI: 10.3389/fpls.2022.899738

Experimental method

X-RAY DIFFRACTION (3 Å)