View source for 6swr


==Crystal structure of the lysosomal potassium channel MtTMEM175 T38A mutant soaked with zinc==
<StructureSection load='6swr' size='340' side='right'caption='[[6swr]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== 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>
</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='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='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'>[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>
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6swr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Camelus glama]]
[[Category: Flexibacter tractuosus]]
[[Category: Large Structures]]
[[Category: Brunner, J D]]
[[Category: Jakob, R P]]
[[Category: Maier, T]]
[[Category: Moroni, A]]
[[Category: Neldner, Y]]
[[Category: Schenck, S]]
[[Category: Schulze, T]]
[[Category: Thiel, G]]
[[Category: Lysosome]]
[[Category: Parkinson disease]]
[[Category: Potassium channel]]
[[Category: Tmem175]]
[[Category: Transport protein]]