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==Crystal structure of peptide transporter POT (E310Q mutant) in complex with alafosfalin==
==Crystal structure of peptide transporter POT (E310Q mutant) in complex with alafosfalin==
<StructureSection load='4ikz' size='340' side='right'caption='[[4ikz]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='4ikz' size='340' side='right'caption='[[4ikz]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ikz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IKZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IKZ FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IKZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IKZ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AFS:N-[(1R)-1-PHOSPHONOETHYL]-L-ALANINAMIDE'>AFS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</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=4ikz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ikz OCA], [https://pdbe.org/4ikz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ikz RCSB], [https://www.ebi.ac.uk/pdbsum/4ikz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ikz ProSAT]</span></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4ikv|4ikv]], [[4ikw|4ikw]], [[4ikx|4ikx]], [[4iky|4iky]]</div></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=4ikz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ikz OCA], [https://pdbe.org/4ikz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ikz RCSB], [https://www.ebi.ac.uk/pdbsum/4ikz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ikz ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Proton-dependent oligopeptide transporters (POTs) are major facilitator superfamily (MFS) proteins that mediate the uptake of peptides and peptide-like molecules, using the inwardly directed H+ gradient across the membrane. The human POT family transporter peptide transporter 1 is present in the brush border membrane of the small intestine and is involved in the uptake of nutrient peptides and drug molecules such as beta-lactam antibiotics. Although previous studies have provided insight into the overall structure of the POT family transporters, the question of how transport is coupled to both peptide and H+ binding remains unanswered. Here we report the high-resolution crystal structures of a bacterial POT family transporter, including its complex with a dipeptide analog, alafosfalin. These structures revealed the key mechanistic and functional roles for a conserved glutamate residue (Glu310) in the peptide binding site. Integrated structural, biochemical, and computational analyses suggested a mechanism for H+-coupled peptide symport in which protonated Glu310 first binds the carboxyl group of the peptide substrate. The deprotonation of Glu310 in the inward open state triggers the release of the bound peptide toward the intracellular space and salt bridge formation between Glu310 and Arg43 to induce the state transition to the occluded conformation.
Structural basis for dynamic mechanism of proton-coupled symport by the peptide transporter POT.,Doki S, Kato HE, Solcan N, Iwaki M, Koyama M, Hattori M, Iwase N, Tsukazaki T, Sugita Y, Kandori H, Newstead S, Ishitani R, Nureki O Proc Natl Acad Sci U S A. 2013 Jun 24. PMID:23798427<ref>PMID:23798427</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ikz" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
*[[ABC transporter 3D structures|ABC transporter 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Doki, S]]
[[Category: Doki S]]
[[Category: Ishitani, R]]
[[Category: Ishitani R]]
[[Category: Kato, H E]]
[[Category: Kato HE]]
[[Category: Nureki, O]]
[[Category: Nureki O]]
[[Category: Major facilitator superfamily]]
[[Category: Transport protein]]

Revision as of 13:44, 31 August 2022

Crystal structure of peptide transporter POT (E310Q mutant) in complex with alafosfalinCrystal structure of peptide transporter POT (E310Q mutant) in complex with alafosfalin

Structural highlights

Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

See Also

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