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==Structural insights into substrate recognition in proton dependent oligopeptide transporters== | |||
<StructureSection load='4lep' size='340' side='right' caption='[[4lep]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4lep]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Shewanella_oneidensis_mr-1 Shewanella oneidensis mr-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LEP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LEP FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AFS:N-[(1R)-1-PHOSPHONOETHYL]-L-ALANINAMIDE'>AFS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SO_1277 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=211586 Shewanella oneidensis MR-1])</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=4lep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lep OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lep RCSB], [http://www.ebi.ac.uk/pdbsum/4lep PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Short-chain peptides are transported across membranes through promiscuous proton-dependent oligopeptide transporters (POTs)-a subfamily of the major facilitator superfamily (MFS). The human POTs, PEPT1 and PEPT2, are also involved in the absorption of various drugs in the gut as well as transport to target cells. Here, we present a structure of an oligomeric POT transporter from Shewanella oneidensis (PepTSo2), which was crystallized in the inward open conformation in complex with the peptidomimetic alafosfalin. All ligand-binding residues are highly conserved and the structural insights presented here are therefore likely to also apply to human POTs. | |||
Structural insights into substrate recognition in proton-dependent oligopeptide transporters.,Guettou F, Quistgaard EM, Tresaugues L, Moberg P, Jegerschold C, Zhu L, Jong AJ, Nordlund P, Low C EMBO Rep. 2013 Jul 19. doi: 10.1038/embor.2013.107. PMID:23867627<ref>PMID:23867627</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Shewanella oneidensis mr-1]] | [[Category: Shewanella oneidensis mr-1]] | ||
[[Category: Guettou, F | [[Category: Guettou, F]] | ||
[[Category: Jegerschold, C | [[Category: Jegerschold, C]] | ||
[[Category: Jong, A J | [[Category: Jong, A J]] | ||
[[Category: Low, C | [[Category: Low, C]] | ||
[[Category: Moberg, P | [[Category: Moberg, P]] | ||
[[Category: Nordlund, P | [[Category: Nordlund, P]] | ||
[[Category: Quistgaard, E M | [[Category: Quistgaard, E M]] | ||
[[Category: Tresaugues, L | [[Category: Tresaugues, L]] | ||
[[Category: Zhu, L | [[Category: Zhu, L]] | ||
[[Category: Membrane protein]] | [[Category: Membrane protein]] | ||
[[Category: Mfs superfamily]] | [[Category: Mfs superfamily]] | ||
[[Category: Peptide transporter]] | [[Category: Peptide transporter]] | ||
[[Category: Tranport protein]] | [[Category: Tranport protein]] | ||
Revision as of 17:58, 5 January 2015
Structural insights into substrate recognition in proton dependent oligopeptide transportersStructural insights into substrate recognition in proton dependent oligopeptide transporters
Structural highlights
Publication Abstract from PubMedShort-chain peptides are transported across membranes through promiscuous proton-dependent oligopeptide transporters (POTs)-a subfamily of the major facilitator superfamily (MFS). The human POTs, PEPT1 and PEPT2, are also involved in the absorption of various drugs in the gut as well as transport to target cells. Here, we present a structure of an oligomeric POT transporter from Shewanella oneidensis (PepTSo2), which was crystallized in the inward open conformation in complex with the peptidomimetic alafosfalin. All ligand-binding residues are highly conserved and the structural insights presented here are therefore likely to also apply to human POTs. Structural insights into substrate recognition in proton-dependent oligopeptide transporters.,Guettou F, Quistgaard EM, Tresaugues L, Moberg P, Jegerschold C, Zhu L, Jong AJ, Nordlund P, Low C EMBO Rep. 2013 Jul 19. doi: 10.1038/embor.2013.107. PMID:23867627[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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