4tpj

From Proteopedia

(Difference between revisions)

Current revision

Selectivity mechanism of a bacterial homologue of the human drug peptide transporters PepT1 and PepT2

Structural highlights

4tpj is a 4 chain structure with sequence from Shewanella oneidensis MR-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.201Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8EHE6_SHEON

Publication Abstract from PubMed

Peptide transporters of the PepT family have key roles in the transport of di- and tripeptides across membranes as well as in the absorption of orally administered drugs in the small intestine. We have determined structures of a PepT transporter from Shewanella oneidensis (PepTSo2) in complex with three different peptides. The peptides bind in a large cavity lined by residues that are highly conserved in human PepT1 and PepT2. The bound peptides adopt extended conformations with their N termini clamped into a conserved polar pocket. A positively charged patch allows differential interactions with the C-terminal carboxylates of di- and tripeptides. Here we identify three pockets for peptide side chain interactions, and our binding studies define differential roles of these pockets for the recognition of different subtypes of peptide side chains.

Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2.,Guettou F, Quistgaard EM, Raba M, Moberg P, Low C, Nordlund P Nat Struct Mol Biol. 2014 Aug;21(8):728-31. doi: 10.1038/nsmb.2860. Epub 2014 Jul, 27. PMID:25064511^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Guettou F, Quistgaard EM, Raba M, Moberg P, Low C, Nordlund P. Selectivity mechanism of a bacterial homolog of the human drug-peptide transporters PepT1 and PepT2. Nat Struct Mol Biol. 2014 Aug;21(8):728-31. doi: 10.1038/nsmb.2860. Epub 2014 Jul, 27. PMID:25064511 doi:http://dx.doi.org/10.1038/nsmb.2860

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4tpj"

@@ Line 3: / Line 3: @@
 <StructureSection load='4tpj' size='340' side='right'caption='[[4tpj]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4tpj]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TPJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TPJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4tpj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_oneidensis_MR-1 Shewanella oneidensis MR-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TPJ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.201&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tph|4tph]], [[4tpg|4tpg]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tpj OCA], [http://pdbe.org/4tpj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tpj RCSB], [http://www.ebi.ac.uk/pdbsum/4tpj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tpj ProSAT]</span></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=4tpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tpj OCA], [https://pdbe.org/4tpj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tpj RCSB], [https://www.ebi.ac.uk/pdbsum/4tpj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tpj ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q8EHE6_SHEON Q8EHE6_SHEON]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 21: @@
 ==See Also==
-*[[Symporter|Symporter]]
+*[[Symporter 3D structures|Symporter 3D structures]]
 == References ==
 <references/>
@@ Line 25: / Line 27: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Guettou, F]]
+[[Category: Shewanella oneidensis MR-1]]
-[[Category: Low, C]]
+[[Category: Guettou F]]
-[[Category: Moberg, P]]
+[[Category: Low C]]
-[[Category: Nordlund, P]]
+[[Category: Moberg P]]
-[[Category: Quistgaard, E]]
+[[Category: Nordlund P]]
-[[Category: Raba, M]]
+[[Category: Quistgaard E]]
-[[Category: Complex]]
+[[Category: Raba M]]
-[[Category: Membrane protein]]
-[[Category: Secondary active transporter]]

4tpj

From Proteopedia

Current revision

Selectivity mechanism of a bacterial homologue of the human drug peptide transporters PepT1 and PepT2

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox