6swr

<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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</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>

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== 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.

 

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== References ==

[[Category: Camelus glama]]

[[Category: Flexibacter tractuosus]]

[[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: Transport protein]]