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6qv2
From Proteopedia
(Difference between revisions)
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<StructureSection load='6qv2' size='340' side='right'caption='[[6qv2]], [[Resolution|resolution]] 4.23Å' scene=''> | <StructureSection load='6qv2' size='340' side='right'caption='[[6qv2]], [[Resolution|resolution]] 4.23Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6qv2]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QV2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QV2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6qv2]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Alpaca Alpaca] and [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QV2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QV2 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGS:PHOSPHOTHIOPHOSPHORIC+ACID-ADENYLATE+ESTER'>AGS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
| + | <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=243274 THEMA]), TM_0288 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</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=6qv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qv2 OCA], [http://pdbe.org/6qv2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qv2 RCSB], [http://www.ebi.ac.uk/pdbsum/6qv2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qv2 ProSAT]</span></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=6qv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qv2 OCA], [http://pdbe.org/6qv2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qv2 RCSB], [http://www.ebi.ac.uk/pdbsum/6qv2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qv2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | ABC exporters harness the energy of ATP to pump substrates across membranes. Extracellular gate opening and closure are key steps of the transport cycle, but the underlying mechanism is poorly understood. Here, we generated a synthetic single domain antibody (sybody) that recognizes the heterodimeric ABC exporter TM287/288 exclusively in the presence of ATP, which was essential to solve a 3.2 A crystal structure of the outward-facing transporter. The sybody binds to an extracellular wing and strongly inhibits ATPase activity by shifting the transporter's conformational equilibrium towards the outward-facing state, as shown by double electron-electron resonance (DEER). Mutations that facilitate extracellular gate opening result in a comparable equilibrium shift and strongly reduce ATPase activity and drug transport. Using the sybody as conformational probe, we demonstrate that efficient extracellular gate closure is required to dissociate the NBD dimer after ATP hydrolysis to reset the transporter back to its inward-facing state. | ||
| + | |||
| + | The extracellular gate shapes the energy profile of an ABC exporter.,Hutter CAJ, Timachi MH, Hurlimann LM, Zimmermann I, Egloff P, Goddeke H, Kucher S, Stefanic S, Karttunen M, Schafer LV, Bordignon E, Seeger MA Nat Commun. 2019 May 21;10(1):2260. doi: 10.1038/s41467-019-09892-6. PMID:31113958<ref>PMID:31113958</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6qv2" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Alpaca]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Thema]] | ||
[[Category: Egloff, P]] | [[Category: Egloff, P]] | ||
[[Category: Huerlimann, L M]] | [[Category: Huerlimann, L M]] | ||
Current revision
Structure of ATPgS-bound outward-facing TM287/288 in complex with nanobody Nb_TM#2
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