4r73
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4r73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r73 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r73 RCSB], [http://www.ebi.ac.uk/pdbsum/4r73 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4r73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r73 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r73 RCSB], [http://www.ebi.ac.uk/pdbsum/4r73 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Efficient acquisition of extracellular nutrients is essential for bacterial pathogenesis, however the identities and mechanisms for transport of many of these substrates remain unclear. Here, we investigate the predicted iron-binding transporter AfuABC and its role in bacterial pathogenesis in vivo. By crystallographic, biophysical and in vivo approaches, we show that AfuABC is in fact a cyclic hexose/heptose-phosphate transporter with high selectivity and specificity for a set of ubiquitous metabolites (glucose-6-phosphate, fructose-6-phosphate and sedoheptulose-7-phosphate). AfuABC is conserved across a wide range of bacterial genera, including the enteric pathogens EHEC O157:H7 and its murine-specific relative Citrobacter rodentium, where it lies adjacent to genes implicated in sugar sensing and acquisition. C. rodentium DeltaafuA was significantly impaired in an in vivo murine competitive assay as well as its ability to transmit infection from an afflicted to a naive murine host. Sugar-phosphates were present in normal and infected intestinal mucus and stool samples, indicating that these metabolites are available within the intestinal lumen for enteric bacteria to import during infection. Our study shows that AfuABC-dependent uptake of sugar-phosphates plays a critical role during enteric bacterial infection and uncovers previously unrecognized roles for these metabolites as important contributors to successful pathogenesis. | ||
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+ | Active Transport of Phosphorylated Carbohydrates Promotes Intestinal Colonization and Transmission of a Bacterial Pathogen.,Sit B, Crowley SM, Bhullar K, Lai CC, Tang C, Hooda Y, Calmettes C, Khambati H, Ma C, Brumell JH, Schryvers AB, Vallance BA, Moraes TF PLoS Pathog. 2015 Aug 21;11(8):e1005107. doi: 10.1371/journal.ppat.1005107., eCollection 2015 Aug. PMID:26295949<ref>PMID:26295949</ref> | ||
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+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 06:37, 2 September 2015
Structure of the periplasmic binding protein AfuA from Actinobacillus pleuropneumoniae (endogenous glucose-6-phosphate and mannose-6-phosphate bound)
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