4rp8 | pdb_00004rp8

Bacterial vitamin C transporter UlaA/SgaT in P21 form

spinqualitylabelsall models 4rp8, resolution 2.36Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4rp8 is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.359Å Ligands: ASC, BNG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ULAA_ECOLI The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active-transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. This system is involved in ascorbate transport. Publication Abstract from PubMed 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 coli in two conformations at 1.65-A and 2.35-A 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. Crystal structure of a phosphorylation-coupled vitamin C transporter.,Luo P, Yu X, Wang W, Fan S, Li X, Wang J Nat Struct Mol Biol. 2015 Feb 16. doi: 10.1038/nsmb.2975. PMID:25686089 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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