7jm7: Difference between revisions
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The entry | ==Structure of human CLC-7/OSTM1 complex== | ||
<StructureSection load='7jm7' size='340' side='right'caption='[[7jm7]], [[Resolution|resolution]] 2.82Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7jm7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JM7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JM7 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.82Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0J1:(2R)-3-{[(R)-hydroxy{[(1S,2R,3S,4S,5R,6R)-2,3,4,6-tetrahydroxy-5-(phosphonooxy)cyclohexyl]oxy}phosphoryl]oxy}propane-1,2-diyl+dinonanoate'>0J1</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=7jm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jm7 OCA], [https://pdbe.org/7jm7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jm7 RCSB], [https://www.ebi.ac.uk/pdbsum/7jm7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jm7 ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/OSTM1_HUMAN OSTM1_HUMAN] Infantile osteopetrosis with neuroaxonal dysplasia. The disease is caused by variants affecting the gene represented in this entry. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/OSTM1_HUMAN OSTM1_HUMAN] Required for osteoclast and melanocyte maturation and function.<ref>PMID:21527911</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The chloride-proton exchanger CLC-7 plays critical roles in lysosomal homeostasis and bone regeneration and its mutation can lead to osteopetrosis, lysosomal storage disease and neurological disorders. In lysosomes and the ruffled border of osteoclasts, CLC-7 requires a beta-subunit, OSTM1, for stability and activity. Here, we present electron cryomicroscopy structures of CLC-7 in occluded states by itself and in complex with OSTM1, determined at resolutions up to 2.8 A. In the complex, the luminal surface of CLC-7 is entirely covered by a dimer of the heavily glycosylated and disulfide-bonded OSTM1, which serves to protect CLC-7 from the degradative environment of the lysosomal lumen. OSTM1 binding does not induce large-scale rearrangements of CLC-7, but does have minor effects on the conformation of the ion-conduction pathway, potentially contributing to its regulatory role. These studies provide insights into the role of OSTM1 and serve as a foundation for understanding the mechanisms of CLC-7 regulation. | |||
Cryo-EM structure of the lysosomal chloride-proton exchanger CLC-7 in complex with OSTM1.,Schrecker M, Korobenko J, Hite RK Elife. 2020 Aug 4;9. pii: 59555. doi: 10.7554/eLife.59555. PMID:32749217<ref>PMID:32749217</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Hite | <div class="pdbe-citations 7jm7" style="background-color:#fffaf0;"></div> | ||
[[Category: Schrecker | |||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Hite R]] | |||
[[Category: Schrecker M]] | |||
Latest revision as of 11:53, 17 October 2024
Structure of human CLC-7/OSTM1 complexStructure of human CLC-7/OSTM1 complex
Structural highlights
DiseaseOSTM1_HUMAN Infantile osteopetrosis with neuroaxonal dysplasia. The disease is caused by variants affecting the gene represented in this entry. FunctionOSTM1_HUMAN Required for osteoclast and melanocyte maturation and function.[1] Publication Abstract from PubMedThe chloride-proton exchanger CLC-7 plays critical roles in lysosomal homeostasis and bone regeneration and its mutation can lead to osteopetrosis, lysosomal storage disease and neurological disorders. In lysosomes and the ruffled border of osteoclasts, CLC-7 requires a beta-subunit, OSTM1, for stability and activity. Here, we present electron cryomicroscopy structures of CLC-7 in occluded states by itself and in complex with OSTM1, determined at resolutions up to 2.8 A. In the complex, the luminal surface of CLC-7 is entirely covered by a dimer of the heavily glycosylated and disulfide-bonded OSTM1, which serves to protect CLC-7 from the degradative environment of the lysosomal lumen. OSTM1 binding does not induce large-scale rearrangements of CLC-7, but does have minor effects on the conformation of the ion-conduction pathway, potentially contributing to its regulatory role. These studies provide insights into the role of OSTM1 and serve as a foundation for understanding the mechanisms of CLC-7 regulation. Cryo-EM structure of the lysosomal chloride-proton exchanger CLC-7 in complex with OSTM1.,Schrecker M, Korobenko J, Hite RK Elife. 2020 Aug 4;9. pii: 59555. doi: 10.7554/eLife.59555. PMID:32749217[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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