4tpj: Difference between revisions
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New page: '''Unreleased structure''' The entry 4tpj is ON HOLD Authors: Fatma Guettou, Esben Quistgaard, Michael Raba, Per Moberg, Christian Low, Par Nordlund Description: |
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==Selectivity mechanism of a bacterial homologue of the human drug peptide transporters PepT1 and PepT2== | |||
<StructureSection load='4tpj' size='340' side='right'caption='[[4tpj]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4tpj]] is a 4 chain structure with sequence from [https://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=4TPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TPJ FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.201Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4tpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tpj OCA], [https://pdbe.org/4tpj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tpj RCSB], [https://www.ebi.ac.uk/pdbsum/4tpj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tpj ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8EHE6_SHEON Q8EHE6_SHEON] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Peptide transporters of the PepT family have key roles in the transport of di- and tripeptides across membranes as well as in the absorption of orally administered drugs in the small intestine. We have determined structures of a PepT transporter from Shewanella oneidensis (PepTSo2) in complex with three different peptides. The peptides bind in a large cavity lined by residues that are highly conserved in human PepT1 and PepT2. The bound peptides adopt extended conformations with their N termini clamped into a conserved polar pocket. A positively charged patch allows differential interactions with the C-terminal carboxylates of di- and tripeptides. Here we identify three pockets for peptide side chain interactions, and our binding studies define differential roles of these pockets for the recognition of different subtypes of peptide side chains. | |||
Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2.,Guettou F, Quistgaard EM, Raba M, Moberg P, Low C, Nordlund P Nat Struct Mol Biol. 2014 Aug;21(8):728-31. doi: 10.1038/nsmb.2860. Epub 2014 Jul, 27. PMID:25064511<ref>PMID:25064511</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4tpj" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Symporter 3D structures|Symporter 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Shewanella oneidensis MR-1]] | |||
[[Category: Guettou F]] | |||
[[Category: Low C]] | |||
[[Category: Moberg P]] | |||
[[Category: Nordlund P]] | |||
[[Category: Quistgaard E]] | |||
[[Category: Raba M]] | |||
Latest revision as of 15:24, 20 December 2023
Selectivity mechanism of a bacterial homologue of the human drug peptide transporters PepT1 and PepT2Selectivity mechanism of a bacterial homologue of the human drug peptide transporters PepT1 and PepT2
Structural highlights
FunctionPublication Abstract from PubMedPeptide transporters of the PepT family have key roles in the transport of di- and tripeptides across membranes as well as in the absorption of orally administered drugs in the small intestine. We have determined structures of a PepT transporter from Shewanella oneidensis (PepTSo2) in complex with three different peptides. The peptides bind in a large cavity lined by residues that are highly conserved in human PepT1 and PepT2. The bound peptides adopt extended conformations with their N termini clamped into a conserved polar pocket. A positively charged patch allows differential interactions with the C-terminal carboxylates of di- and tripeptides. Here we identify three pockets for peptide side chain interactions, and our binding studies define differential roles of these pockets for the recognition of different subtypes of peptide side chains. Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2.,Guettou F, Quistgaard EM, Raba M, Moberg P, Low C, Nordlund P Nat Struct Mol Biol. 2014 Aug;21(8):728-31. doi: 10.1038/nsmb.2860. Epub 2014 Jul, 27. PMID:25064511[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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