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| <StructureSection load='6swr' size='340' side='right'caption='[[6swr]], [[Resolution|resolution]] 3.20Å' scene=''> | | <StructureSection load='6swr' size='340' side='right'caption='[[6swr]], [[Resolution|resolution]] 3.20Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6swr]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Camelus_glama Camelus glama] and [http://en.wikipedia.org/wiki/Flexibacter_tractuosus Flexibacter tractuosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SWR OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6SWR FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SWR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SWR FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</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]] 3.2Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6hd8|6hd8]], [[6hd9|6hd9]], [[6hda|6hda]], [[6hdb|6hdb]], [[6hdc|6hdc]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">malE, b4034, JW3994 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9844 Camelus glama]), Ftrac_2467 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=643867 Flexibacter tractuosus])</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=6swr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6swr OCA], [https://pdbe.org/6swr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6swr RCSB], [https://www.ebi.ac.uk/pdbsum/6swr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6swr ProSAT]</span></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=6swr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6swr OCA], [http://pdbe.org/6swr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6swr RCSB], [http://www.ebi.ac.uk/pdbsum/6swr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6swr ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The TMEM175 family constitutes recently discovered K(+) channels that are important for autophagosome turnover and lysosomal pH regulation and are associated with the early onset of Parkinson Disease. TMEM175 channels lack a P-loop selectivity filter, a hallmark of all known K(+) channels, raising the question how selectivity is achieved. Here, we report the X-ray structure of a closed bacterial TMEM175 channel in complex with a nanobody fusion-protein disclosing bound K(+) ions. Our analysis revealed that a highly conserved layer of threonine residues in the pore conveys a basal K(+) selectivity. An additional layer comprising two serines in human TMEM175 increases selectivity further and renders this channel sensitive to 4-aminopyridine and Zn(2+). Our findings suggest that large hydrophobic side chains occlude the pore, forming a physical gate, and that channel opening by iris-like motions simultaneously relocates the gate and exposes the otherwise concealed selectivity filter to the pore lumen.
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| Structural basis for ion selectivity in TMEM175 K(+) channels.,Brunner JD, Jakob RP, Schulze T, Neldner Y, Moroni A, Thiel G, Maier T, Schenck S Elife. 2020 Apr 8;9. pii: 53683. doi: 10.7554/eLife.53683. PMID:32267231<ref>PMID:32267231</ref>
| | ==See Also== |
| | | *[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6swr" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Camelus glama]]
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| [[Category: Flexibacter tractuosus]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Brunner, J D]] | | [[Category: Brunner JD]] |
| [[Category: Jakob, R P]] | | [[Category: Jakob RP]] |
| [[Category: Maier, T]] | | [[Category: Maier T]] |
| [[Category: Moroni, A]] | | [[Category: Moroni A]] |
| [[Category: Neldner, Y]] | | [[Category: Neldner Y]] |
| [[Category: Schenck, S]] | | [[Category: Schenck S]] |
| [[Category: Schulze, T]] | | [[Category: Schulze T]] |
| [[Category: Thiel, G]] | | [[Category: Thiel G]] |
| [[Category: Lysosome]]
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| [[Category: Parkinson disease]]
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| [[Category: Potassium channel]]
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| [[Category: Tmem175]]
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| [[Category: Transport protein]]
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