3qf4

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==Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation==
==Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation==
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<StructureSection load='3qf4' size='340' side='right' caption='[[3qf4]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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<StructureSection load='3qf4' size='340' side='right'caption='[[3qf4]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3qf4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QF4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QF4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3qf4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QF4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QF4 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=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qf5|3qf5]]</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=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM_0287 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]), TM_0288 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])</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=3qf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qf4 OCA], [https://pdbe.org/3qf4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qf4 RCSB], [https://www.ebi.ac.uk/pdbsum/3qf4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qf4 ProSAT]</span></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=3qf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qf4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qf4 RCSB], [http://www.ebi.ac.uk/pdbsum/3qf4 PDBsum]</span></td></tr>
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</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/Q9WYC3_THEMA Q9WYC3_THEMA]
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ATP-binding cassette (ABC) transporters shuttle a wide variety of molecules across cell membranes by alternating between inward- and outward-facing conformations, harnessing the energy of ATP binding and hydrolysis at their nucleotide binding domains (NBDs). Here we present the 2.9-A crystal structure of the heterodimeric ABC transporter TM287-TM288 (TM287/288) from Thermotoga maritima in its inward-facing state. In contrast to previous studies, we found that the NBDs only partially separate, remaining in contact through an interface involving conserved motifs that connect the two ATP hydrolysis sites. We observed AMP-PNP binding to the degenerate catalytic site, which deviates from the consensus sequence in the same positions as the eukaryotic homologs CFTR and TAP1-TAP2 (TAP1/2). The TM287/288 structure provides unprecedented insights into the mechanism of heterodimeric ABC exporters and will enable future studies on this large transporter superfamily.
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Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation.,Hohl M, Briand C, Grutter MG, Seeger MA Nat Struct Mol Biol. 2012 Mar 25;19(4):395-402. doi: 10.1038/nsmb.2267. PMID:22447242<ref>PMID:22447242</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 ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
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[[Category: Briand, C]]
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[[Category: Briand C]]
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[[Category: Gruetter, M G]]
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[[Category: Gruetter MG]]
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[[Category: Hohl, M]]
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[[Category: Hohl M]]
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[[Category: Seeger, M A]]
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[[Category: Seeger MA]]
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[[Category: Multidrug transporter]]
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[[Category: Transport protein]]
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Current revision

Crystal structure of a heterodimeric ABC transporter in its inward-facing conformation

PDB ID 3qf4

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