期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 22, 期 3, 页码 238-241出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2975
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资金
- Ministry of Science and Technology of China [2011CB911102, 2015CB910104]
- Tsinghua University 985 Phase II funds
- National Natural Science Foundation of China [31321062]
- Beijing Municipal Commissions of Education and Science and Technology
- Gordon and Betty Moore Foundation Fellow of the Life Sciences Research Foundation
Bacteria use vitamin C (L-ascorbic acid) as a carbon source under anaerobic conditions. The phosphoenolpyruvate-dependent phosphotransferase system (PTS), comprising a transporter (UlaA), a IIB-like enzyme (UlaB) and a IIA-like enzyme (UlaC), is required for the anaerobic uptake of vitamin C and its phosphorylation to L-ascorbate 6-phosphate. Here, we present the crystal structures of vitamin C-bound UlaA from Escherichia coil in two conformations at 1.65-angstrom and 2.35-angstrom resolution. UlaA forms a homodimer and exhibits a new fold. Each UlaA protomer consists of 11 transmembrane segments arranged into a 'V-motif' domain and a 'core' domain. The V motifs form the interface between the two protomers, and the core-domain residues coordinate vitamin C. The alternating access of the substrate from the opposite side of the cell membrane may be achieved through rigid-body rotation of the core relative to the V motif.
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