4lds

</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=4lds FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lds OCA], [https://pdbe.org/4lds PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lds RCSB], [https://www.ebi.ac.uk/pdbsum/4lds PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lds ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Glucose transporters are required to bring glucose into cells, where it is an essential energy source and precursor in protein and lipid synthesis. These transporters are involved in important common diseases such as cancer and diabetes. Here, we report the crystal structure of the Staphylococcus epidermidis glucose/H(+) symporter in an inward-facing conformation at 3.2-A resolution. The Staphylococcus epidermidis glucose/H(+) symporter is homologous to human glucose transporters, is very specific and has high avidity for glucose, and is inhibited by the human glucose transport inhibitors cytochalasin B, phloretin, and forskolin. On the basis of the crystal structure in conjunction with mutagenesis and functional studies, we propose a mechanism for glucose/H(+) symport and discuss the symport mechanism versus facilitated diffusion.

Crystal structure of a glucose/H+ symporter and its mechanism of action.,Iancu CV, Zamoon J, Woo SB, Aleshin A, Choe JY Proc Natl Acad Sci U S A. 2013 Oct 29;110(44):17862-7. doi:, 10.1073/pnas.1311485110. Epub 2013 Oct 14. PMID:24127585<ref>PMID:24127585</ref>

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

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