5oxp: Difference between revisions
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==PepTSt in occluded conformation with phosphate ion bound== | ==PepTSt in occluded conformation with phosphate ion bound== | ||
<StructureSection load='5oxp' size='340' side='right' caption='[[5oxp]], [[Resolution|resolution]] 2.37Å' scene=''> | <StructureSection load='5oxp' size='340' side='right'caption='[[5oxp]], [[Resolution|resolution]] 2.37Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5oxp]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5oxp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_thermophilus_LMG_18311 Streptococcus thermophilus LMG 18311]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OXP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=78M:(2S)-2,3-DIHYDROXYPROPYL(7Z)-PENTADEC-7-ENOATE'>78M</scene>, <scene name='pdbligand=78N:(2R)-2,3-DIHYDROXYPROPYL(7Z)-PENTADEC-7-ENOATE'>78N</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.372Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=78M:(2S)-2,3-DIHYDROXYPROPYL(7Z)-PENTADEC-7-ENOATE'>78M</scene>, <scene name='pdbligand=78N:(2R)-2,3-DIHYDROXYPROPYL(7Z)-PENTADEC-7-ENOATE'>78N</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5oxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oxp OCA], [https://pdbe.org/5oxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oxp RCSB], [https://www.ebi.ac.uk/pdbsum/5oxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oxp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5M4H8_STRT2 Q5M4H8_STRT2] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 5oxp" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5oxp" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Symporter 3D structures|Symporter 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptococcus thermophilus LMG 18311]] | ||
[[Category: | [[Category: Loew C]] | ||
[[Category: | [[Category: Martinez Molledo M]] | ||
[[Category: | [[Category: Quistgaard EM]] | ||
Latest revision as of 04:27, 28 December 2023
PepTSt in occluded conformation with phosphate ion boundPepTSt in occluded conformation with phosphate ion bound
Structural highlights
FunctionPublication Abstract from PubMedProton-dependent oligopeptide transporters (POTs) are important for uptake of dietary di- and tripeptides in many organisms, and in humans are also involved in drug absorption. These transporters accept a wide range of substrates, but the structural basis for how different peptide side chains are accommodated has so far remained obscure. Twenty-eight peptides were screened for binding to PepTSt from Streptococcus thermophilus, and structures were determined of PepTSt in complex with four physicochemically diverse dipeptides, which bind with millimolar affinity: Ala-Leu, Phe-Ala, Ala-Gln, and Asp-Glu. The structures show that PepTSt can adapt to different peptide side chains through movement of binding site residues and water molecules, and that a good fit can be further aided by adjustment of the position of the peptide itself. Finally, structures were also determined in complex with adventitiously bound HEPES, polyethylene glycol, and phosphate molecules, which further underline the adaptability of the binding site. Multispecific Substrate Recognition in a Proton-Dependent Oligopeptide Transporter.,Martinez Molledo M, Quistgaard EM, Flayhan A, Pieprzyk J, Low C Structure. 2018 Mar 6;26(3):467-476.e4. doi: 10.1016/j.str.2018.01.005. Epub 2018, Feb 8. PMID:29429879[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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