6hd8: Difference between revisions
New page: '''Unreleased structure''' The entry 6hd8 is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==Crystal structure of the potassium channel MtTMEM175 in complex with a Nanobody-MBP fusion protein== | ||
<StructureSection load='6hd8' size='340' side='right'caption='[[6hd8]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6hd8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12], [https://en.wikipedia.org/wiki/Lama_glama Lama glama] and [https://en.wikipedia.org/wiki/Marivirga_tractuosa_DSM_4126 Marivirga tractuosa DSM 4126]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HD8 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]] 2.4Å</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>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</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=6hd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hd8 OCA], [https://pdbe.org/6hd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hd8 RCSB], [https://www.ebi.ac.uk/pdbsum/6hd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hd8 ProSAT]</span></td></tr> | |||
</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> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6hd8" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Maltose-binding protein 3D structures|Maltose-binding protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Lama glama]] | |||
[[Category: Large Structures]] | |||
[[Category: Marivirga tractuosa DSM 4126]] | |||
[[Category: Brunner JD]] | |||
[[Category: Jakob RP]] | |||
[[Category: Maier T]] | |||
[[Category: Moroni A]] | |||
[[Category: Neldner Y]] | |||
[[Category: Schenck S]] | |||
[[Category: Schulze T]] | |||
[[Category: Thiel G]] | |||
Latest revision as of 13:01, 23 October 2024
Crystal structure of the potassium channel MtTMEM175 in complex with a Nanobody-MBP fusion proteinCrystal structure of the potassium channel MtTMEM175 in complex with a Nanobody-MBP fusion protein
Structural highlights
FunctionMALE_ECOLI Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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