3qe7

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==Crystal Structure of Uracil Transporter--UraA==
==Crystal Structure of Uracil Transporter--UraA==
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<StructureSection load='3qe7' size='340' side='right' caption='[[3qe7]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
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<StructureSection load='3qe7' size='340' side='right'caption='[[3qe7]], [[Resolution|resolution]] 2.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qe7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QE7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QE7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qe7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QE7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QE7 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=URA:URACIL'>URA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.781&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uraA, b2497, JW2482 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BNG:B-NONYLGLUCOSIDE'>BNG</scene>, <scene name='pdbligand=URA:URACIL'>URA</scene></td></tr>
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<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=3qe7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qe7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qe7 RCSB], [http://www.ebi.ac.uk/pdbsum/3qe7 PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3qe7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qe7 OCA], [https://pdbe.org/3qe7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qe7 RCSB], [https://www.ebi.ac.uk/pdbsum/3qe7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qe7 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/URAA_ECOLI URAA_ECOLI] Transport of uracil in the cell.<ref>PMID:7721693</ref> <ref>PMID:21423164</ref>
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The nucleobase/ascorbate transporter (NAT) proteins, also known as nucleobase/cation symporter 2 (NCS2) proteins, are responsible for the uptake of nucleobases in all kingdoms of life and for the transport of vitamin C in mammals. Despite functional characterization of the NAT family members in bacteria, fungi and mammals, detailed structural information remains unavailable. Here we report the crystal structure of a representative NAT protein, the Escherichia coli uracil/H(+) symporter UraA, in complex with uracil at a resolution of 2.8 A. UraA has a novel structural fold, with 14 transmembrane segments (TMs) divided into two inverted repeats. A pair of antiparallel beta-strands is located between TM3 and TM10 and has an important role in structural organization and substrate recognition. The structure is spatially arranged into a core domain and a gate domain. Uracil, located at the interface between the two domains, is coordinated mainly by residues from the core domain. Structural analysis suggests that alternating access of the substrate may be achieved through conformational changes of the gate domain.
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Structure and mechanism of the uracil transporter UraA.,Lu F, Li S, Jiang Y, Jiang J, Fan H, Lu G, Deng D, Dang S, Zhang X, Wang J, Yan N Nature. 2011 Apr 14;472(7342):243-6. Epub 2011 Mar 20. PMID:21423164<ref>PMID:21423164</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Escherichia coli K-12]]
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[[Category: Li, S]]
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[[Category: Large Structures]]
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[[Category: Lu, F R]]
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[[Category: Li S]]
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[[Category: Yan, N]]
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[[Category: Lu FR]]
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[[Category: Inner membrane protein]]
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[[Category: Yan N]]
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[[Category: Transport protein]]
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[[Category: Transporter]]
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[[Category: Uraa]]
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[[Category: Uracil permease]]
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[[Category: Uracil transporter]]
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Current revision

Crystal Structure of Uracil Transporter--UraA

PDB ID 3qe7

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