|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5i6c' size='340' side='right'caption='[[5i6c]], [[Resolution|resolution]] 3.70Å' scene=''> | | <StructureSection load='5i6c' size='340' side='right'caption='[[5i6c]], [[Resolution|resolution]] 3.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5i6c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspergillus_nidulans Aspergillus nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I6C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5I6C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5i6c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_nidulans_FGSC_A4 Aspergillus nidulans FGSC A4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I6C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I6C FirstGlance]. <br> |
| - | </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=XAN:XANTHINE'>XAN</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]] 3.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uapA, AN6932 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=227321 Aspergillus nidulans])</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=XAN:XANTHINE'>XAN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5i6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i6c OCA], [http://pdbe.org/5i6c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i6c RCSB], [http://www.ebi.ac.uk/pdbsum/5i6c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i6c 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=5i6c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i6c OCA], [https://pdbe.org/5i6c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i6c RCSB], [https://www.ebi.ac.uk/pdbsum/5i6c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i6c ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/UAPA_EMENI UAPA_EMENI]] Uric acid-xanthine transporter.<ref>PMID:15953615</ref> <ref>PMID:16096268</ref> <ref>PMID:20002879</ref> | + | [https://www.uniprot.org/uniprot/UAPA_EMENI UAPA_EMENI] Uric acid-xanthine transporter.<ref>PMID:15953615</ref> <ref>PMID:16096268</ref> <ref>PMID:20002879</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 26: |
Line 26: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aspergillus nidulans]] | + | [[Category: Aspergillus nidulans FGSC A4]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Alguel, Y]] | + | [[Category: Alguel Y]] |
| - | [[Category: Amillis, S]] | + | [[Category: Amillis S]] |
| - | [[Category: Armstrong, A]] | + | [[Category: Armstrong A]] |
| - | [[Category: Byrne, B]] | + | [[Category: Byrne B]] |
| - | [[Category: Cameron, A D]] | + | [[Category: Cameron AD]] |
| - | [[Category: Capaldi, S]] | + | [[Category: Capaldi S]] |
| - | [[Category: Craven, G]] | + | [[Category: Craven G]] |
| - | [[Category: Diallinas, G]] | + | [[Category: Diallinas G]] |
| - | [[Category: Iwata, S]] | + | [[Category: Iwata S]] |
| - | [[Category: Lambrinidis, G]] | + | [[Category: Lambrinidis G]] |
| - | [[Category: Leung, J]] | + | [[Category: Leung J]] |
| - | [[Category: Mikros, E]] | + | [[Category: Mikros E]] |
| - | [[Category: Scull, N J]] | + | [[Category: Scull NJ]] |
| - | [[Category: Membrane protein eukaryotic uric acid/xanthine h+ symporter]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
UAPA_EMENI Uric acid-xanthine transporter.[1] [2] [3]
Publication Abstract from PubMed
The uric acid/xanthine H(+) symporter, UapA, is a high-affinity purine transporter from the filamentous fungus Aspergillus nidulans. Here we present the crystal structure of a genetically stabilized version of UapA (UapA-G411VDelta1-11) in complex with xanthine. UapA is formed from two domains, a core domain and a gate domain, similar to the previously solved uracil transporter UraA, which belongs to the same family. The structure shows UapA in an inward-facing conformation with xanthine bound to residues in the core domain. Unlike UraA, which was observed to be a monomer, UapA forms a dimer in the crystals with dimer interactions formed exclusively through the gate domain. Analysis of dominant negative mutants is consistent with dimerization playing a key role in transport. We postulate that UapA uses an elevator transport mechanism likely to be shared with other structurally homologous transporters including anion exchangers and prestin.
Structure of eukaryotic purine/H(+) symporter UapA suggests a role for homodimerization in transport activity.,Alguel Y, Amillis S, Leung J, Lambrinidis G, Capaldi S, Scull NJ, Craven G, Iwata S, Armstrong A, Mikros E, Diallinas G, Cameron AD, Byrne B Nat Commun. 2016 Apr 18;7:11336. doi: 10.1038/ncomms11336. PMID:27088252[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Koukaki M, Vlanti A, Goudela S, Pantazopoulou A, Gioule H, Tournaviti S, Diallinas G. The nucleobase-ascorbate transporter (NAT) signature motif in UapA defines the function of the purine translocation pathway. J Mol Biol. 2005 Jul 15;350(3):499-513. PMID:15953615 doi:http://dx.doi.org/10.1016/j.jmb.2005.04.076
- ↑ Goudela S, Karatza P, Koukaki M, Frillingos S, Diallinas G. Comparative substrate recognition by bacterial and fungal purine transporters of the NAT/NCS2 family. Mol Membr Biol. 2005 May-Jun;22(3):263-75. PMID:16096268 doi:http://dx.doi.org/10.1080/09687860500093016
- ↑ Gournas C, Amillis S, Vlanti A, Diallinas G. Transport-dependent endocytosis and turnover of a uric acid-xanthine permease. Mol Microbiol. 2010 Jan;75(1):246-60. doi: 10.1111/j.1365-2958.2009.06997.x. Epub, 2009 Dec 11. PMID:20002879 doi:http://dx.doi.org/10.1111/j.1365-2958.2009.06997.x
- ↑ Alguel Y, Amillis S, Leung J, Lambrinidis G, Capaldi S, Scull NJ, Craven G, Iwata S, Armstrong A, Mikros E, Diallinas G, Cameron AD, Byrne B. Structure of eukaryotic purine/H(+) symporter UapA suggests a role for homodimerization in transport activity. Nat Commun. 2016 Apr 18;7:11336. doi: 10.1038/ncomms11336. PMID:27088252 doi:http://dx.doi.org/10.1038/ncomms11336
|
