6quz
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='6quz' size='340' side='right'caption='[[6quz]], [[Resolution|resolution]] 3.21Å' scene=''> | <StructureSection load='6quz' size='340' side='right'caption='[[6quz]], [[Resolution|resolution]] 3.21Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6quz]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QUZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QUZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6quz]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences] and [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QUZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QUZ 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=6quz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6quz OCA], [http://pdbe.org/6quz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6quz RCSB], [http://www.ebi.ac.uk/pdbsum/6quz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6quz 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=6quz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6quz OCA], [http://pdbe.org/6quz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6quz RCSB], [http://www.ebi.ac.uk/pdbsum/6quz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6quz 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 6quz" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Synthetic construct sequences]] | ||
| + | [[Category: Thema]] | ||
[[Category: Egloff, P]] | [[Category: Egloff, P]] | ||
[[Category: Huerlimann, L M]] | [[Category: Huerlimann, L M]] | ||
Revision as of 23:13, 5 June 2019
Structure of ATPgS-bound outward-facing TM287/288 in complex with sybody Sb_TM35
| |||||||||||
