5tja

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<StructureSection load='5tja' size='340' side='right'caption='[[5tja]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='5tja' size='340' side='right'caption='[[5tja]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5tja]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TJA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TJA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5tja]] is a 1 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=5TJA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TJA FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tjb|5tjb]], [[5tjc|5tjc]]</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MCOLN1, ML4, MSTP080 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5tja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tja OCA], [https://pdbe.org/5tja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tja RCSB], [https://www.ebi.ac.uk/pdbsum/5tja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tja ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tja OCA], [http://pdbe.org/5tja PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tja RCSB], [http://www.ebi.ac.uk/pdbsum/5tja PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tja ProSAT]</span></td></tr>
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</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/MCLN1_HUMAN MCLN1_HUMAN]] Mucolipidosis type 4. The disease is caused by mutations affecting the gene represented in this entry.
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[https://www.uniprot.org/uniprot/MCLN1_HUMAN MCLN1_HUMAN] Mucolipidosis type 4. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MCLN1_HUMAN MCLN1_HUMAN]] Cation channel probably playing a role in the endocytic pathway and in the control of membrane trafficking of proteins and lipids. Could play a major role in Ca(2+) transport regulating lysosomal exocytosis.<ref>PMID:12459486</ref> <ref>PMID:14749347</ref>
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[https://www.uniprot.org/uniprot/MCLN1_HUMAN MCLN1_HUMAN] Cation channel probably playing a role in the endocytic pathway and in the control of membrane trafficking of proteins and lipids. Could play a major role in Ca(2+) transport regulating lysosomal exocytosis.<ref>PMID:12459486</ref> <ref>PMID:14749347</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The activities of organellar ion channels are often regulated by Ca2+ and H+, which are present in high concentrations in many organelles. Here we report a structural element critical for dual Ca2+/pH regulation of TRPML1, a Ca2+-release channel crucial for endolysosomal function. TRPML1 mutations cause mucolipidosis type IV (MLIV), a severe lysosomal storage disorder characterized by neurodegeneration, mental retardation and blindness. We obtained crystal structures of the 213-residue luminal domain of human TRPML1 containing three missense MLIV-causing mutations. This domain forms a tetramer with a highly electronegative central pore formed by a novel luminal pore loop. Cysteine cross-linking and cryo-EM analyses confirmed that this architecture occurs in the full-length channel. Structure-function studies demonstrated that Ca2+ and H+ interact with the luminal pore and exert physiologically important regulation. The MLIV-causing mutations disrupt the luminal-domain structure and cause TRPML1 mislocalization. Our study reveals the structural underpinnings of TRPML1's regulation, assembly and pathogenesis.
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Structural basis of dual Ca2+/pH regulation of the endolysosomal TRPML1 channel.,Li M, Zhang WK, Benvin NM, Zhou X, Su D, Li H, Wang S, Michailidis IE, Tong L, Li X, Yang J Nat Struct Mol Biol. 2017 Mar;24(3):205-213. doi: 10.1038/nsmb.3362. Epub 2017, Jan 23. PMID:28112729<ref>PMID:28112729</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5tja" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Benvin, N M]]
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[[Category: Benvin NM]]
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[[Category: Li, H]]
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[[Category: Li H]]
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[[Category: Li, M]]
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[[Category: Li M]]
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[[Category: Li, X]]
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[[Category: Li X]]
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[[Category: Michailidis, I E]]
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[[Category: Michailidis IE]]
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[[Category: Su, D]]
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[[Category: Su D]]
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[[Category: Tong, L]]
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[[Category: Tong L]]
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[[Category: Wang, S]]
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[[Category: Wang S]]
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[[Category: Yang, J]]
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[[Category: Yang J]]
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[[Category: Zhang, W K]]
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[[Category: Zhang WK]]
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[[Category: Zhou, X]]
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[[Category: Zhou X]]
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[[Category: Calcium and ph regulation]]
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[[Category: Endolysosomal lumen]]
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[[Category: Tetramer]]
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[[Category: Transport protein]]
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Revision as of 15:41, 6 March 2024

I-II linker of TRPML1 channel at pH 6

PDB ID 5tja

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