4rp8

<StructureSection load='4rp8' size='340' side='right'caption='[[4rp8]], [[Resolution|resolution]] 2.36&Aring;' scene=''>

<table><tr><td colspan='2'>[[4rp8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RP8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RP8 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASC:ASCORBIC+ACID'>ASC</scene>, <scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rp8 OCA], [https://pdbe.org/4rp8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rp8 RCSB], [https://www.ebi.ac.uk/pdbsum/4rp8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rp8 ProSAT]</span></td></tr>

== Function ==

[[https://www.uniprot.org/uniprot/ULAA_ECOLI 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.

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== 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<ref>PMID:25686089</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Wang, J W]]

[[Category: Vitamin c transporter]]