5oxk: Difference between revisions
New page: '''Unreleased structure''' The entry 5oxk is ON HOLD until Paper Publication Authors: Martinez Molledo, M., Quistgard, E.M., Loew, C. Description: PepTSt in complex with dipeptide Ala-... |
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==PepTSt in complex with dipeptide Ala-Gln== | |||
<StructureSection load='5oxk' size='340' side='right'caption='[[5oxk]], [[Resolution|resolution]] 2.38Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5oxk]] 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=5OXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OXK 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]] 2.38Å</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=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=GLN:GLUTAMINE'>GLN</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'>[https://proteopedia.org/fgij/fg.htm?mol=5oxk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oxk OCA], [https://pdbe.org/5oxk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oxk RCSB], [https://www.ebi.ac.uk/pdbsum/5oxk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oxk ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5M4H8_STRT2 Q5M4H8_STRT2] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Proton-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<ref>PMID:29429879</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5oxk" style="background-color:#fffaf0;"></div> | ||
[[Category: Loew | |||
[[Category: Martinez Molledo | ==See Also== | ||
*[[Symporter 3D structures|Symporter 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus thermophilus LMG 18311]] | |||
[[Category: Loew C]] | |||
[[Category: Martinez Molledo M]] | |||
[[Category: Quistgaard EM]] | |||
Latest revision as of 04:27, 28 December 2023
PepTSt in complex with dipeptide Ala-GlnPepTSt in complex with dipeptide Ala-Gln
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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