4d2d: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (One intermediate revision by the same user not shown) | |||
| Line 3: | Line 3: | ||
<StructureSection load='4d2d' size='340' side='right'caption='[[4d2d]], [[Resolution|resolution]] 2.52Å' scene=''> | <StructureSection load='4d2d' size='340' side='right'caption='[[4d2d]], [[Resolution|resolution]] 2.52Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4d2d]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4d2d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_thermophilus_LMG_18311 Streptococcus thermophilus LMG 18311] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D2D FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.522Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=4d2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d2d OCA], [https://pdbe.org/4d2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d2d RCSB], [https://www.ebi.ac.uk/pdbsum/4d2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d2d 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 == | ||
| Line 19: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[Symporter|Symporter]] | *[[Symporter 3D structures|Symporter 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 25: | Line 27: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptococcus thermophilus LMG 18311]] | ||
[[Category: Brinth | [[Category: Synthetic construct]] | ||
[[Category: Caffrey | [[Category: Brinth A]] | ||
[[Category: Li | [[Category: Caffrey M]] | ||
[[Category: Lyons | [[Category: Li D]] | ||
[[Category: Newstead | [[Category: Lyons JA]] | ||
[[Category: Parker | [[Category: Newstead S]] | ||
[[Category: Shah | [[Category: Parker JL]] | ||
[[Category: Solcan | [[Category: Shah STA]] | ||
[[Category: Solcan N]] | |||
Latest revision as of 15:19, 20 December 2023
Structure of a tri peptide bound POT family peptide transporterStructure of a tri peptide bound POT family peptide transporter
Structural highlights
FunctionPublication Abstract from PubMedAn enigma in the field of peptide transport is the structural basis for ligand promiscuity, as exemplified by PepT1, the mammalian plasma membrane peptide transporter. Here, we present crystal structures of di- and tripeptide-bound complexes of a bacterial homologue of PepT1, which reveal at least two mechanisms for peptide recognition that operate within a single, centrally located binding site. The dipeptide was orientated laterally in the binding site, whereas the tripeptide revealed an alternative vertical binding mode. The co-crystal structures combined with functional studies reveal that biochemically distinct peptide-binding sites likely operate within the POT/PTR family of proton-coupled symporters and suggest that transport promiscuity has arisen in part through the ability of the binding site to accommodate peptides in multiple orientations for transport. Structural basis for polyspecificity in the POT family of proton-coupled oligopeptide transporters.,Lyons JA, Parker JL, Solcan N, Brinth A, Li D, Shah ST, Caffrey M, Newstead S EMBO Rep. 2014 Jun 10. pii: e201338403. PMID:24916388[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||