View source for 4aps


==Crystal structure of a POT family peptide transporter in an inward open conformation.==
<StructureSection load='4aps' size='340' side='right'caption='[[4aps]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4aps]] is a 2 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=4APS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4APS 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]] 3.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</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=4aps FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aps OCA], [https://pdbe.org/4aps PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aps RCSB], [https://www.ebi.ac.uk/pdbsum/4aps PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aps ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5M4H8_STRT2 Q5M4H8_STRT2] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Short chain peptides are actively transported across membranes as an efficient route for dietary protein absorption and for maintaining cellular homeostasis. In mammals, peptide transport occurs via PepT1 and PepT2, which belong to the proton-dependent oligopeptide transporter, or POT family. The recent crystal structure of a bacterial POT transporter confirmed that they belong to the major facilitator superfamily of secondary active transporters. Despite the functional characterization of POT family members in bacteria, fungi and mammals, a detailed model for peptide recognition and transport remains unavailable. In this study, we report the 3.3-A resolution crystal structure and functional characterization of a POT family transporter from the bacterium Streptococcus thermophilus. Crystallized in an inward open conformation the structure identifies a hinge-like movement within the C-terminal half of the transporter that facilitates opening of an intracellular gate controlling access to a central peptide-binding site. Our associated functional data support a model for peptide transport that highlights the importance of salt bridge interactions in orchestrating alternating access within the POT family.

Alternating access mechanism in the POT family of oligopeptide transporters.,Solcan N, Kwok J, Fowler PW, Cameron AD, Drew D, Iwata S, Newstead S EMBO J. 2012 Jun 1. doi: 10.1038/emboj.2012.157. PMID:22659829<ref>PMID:22659829</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4aps" style="background-color:#fffaf0;"></div>

==See Also==
*[[Symporter 3D structures|Symporter 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus thermophilus LMG 18311]]
[[Category: Cameron AD]]
[[Category: Drew D]]
[[Category: Fowler PW]]
[[Category: Iwata S]]
[[Category: Kwok J]]
[[Category: Newstead S]]
[[Category: Solcan N]]