6swr
From Proteopedia
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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'> | + | <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"> | + | <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='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'>[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> | ||
| </table> | </table> | ||
| - | == Function == | ||
| - | [https://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
| - | |||
| - | 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> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 6swr" style="background-color:#fffaf0;"></div> | ||
| ==See Also== | ==See Also== | ||
| *[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]] | *[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
| __TOC__ | __TOC__ | ||
| </StructureSection> | </StructureSection> | ||
| - | [[Category: Escherichia coli K-12]] | ||
| - | [[Category: Lama glama]] | ||
| [[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Marivirga tractuosa DSM 4126]] | ||
| [[Category: Brunner JD]] | [[Category: Brunner JD]] | ||
| [[Category: Jakob RP]] | [[Category: Jakob RP]] | ||
Current revision
Crystal structure of the lysosomal potassium channel MtTMEM175 T38A mutant soaked with zinc
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Categories: Large Structures | Brunner JD | Jakob RP | Maier T | Moroni A | Neldner Y | Schenck S | Schulze T | Thiel G
