5z2h
From Proteopedia
(Difference between revisions)
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==Structure of Dictyostelium discoideum mitochondrial calcium uniporter N-terminal domain(DdMCU-NTD)== | ==Structure of Dictyostelium discoideum mitochondrial calcium uniporter N-terminal domain(DdMCU-NTD)== | ||
- | <StructureSection load='5z2h' size='340' side='right' caption='[[5z2h]], [[Resolution|resolution]] 1.67Å' scene=''> | + | <StructureSection load='5z2h' size='340' side='right'caption='[[5z2h]], [[Resolution|resolution]] 1.67Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[5z2h]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z2H OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[5z2h]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dicdi Dicdi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z2H OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5Z2H FirstGlance]. <br> |
- | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDB0186972 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 DICDI])</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=5z2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z2h OCA], [http://pdbe.org/5z2h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z2h RCSB], [http://www.ebi.ac.uk/pdbsum/5z2h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z2h ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/MCU_DICDI MCU_DICDI]] Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria (PubMed:24889638). Constitutes a pore-forming and calcium-conducting subunit (PubMed:24889638). Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways.[UniProtKB:Q8NE86]<ref>PMID:24889638</ref> | [[http://www.uniprot.org/uniprot/MCU_DICDI MCU_DICDI]] Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria (PubMed:24889638). Constitutes a pore-forming and calcium-conducting subunit (PubMed:24889638). Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of cell death pathways.[UniProtKB:Q8NE86]<ref>PMID:24889638</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The mitochondrial calcium uniporter (MCU) plays a critical role in mitochondrial calcium uptake into the matrix. In metazoans, the uniporter is a tightly regulated multicomponent system, including the pore-forming subunit MCU and several regulators (MICU1, MICU2, and Essential MCU REgulator, EMRE). The calcium-conducting activity of metazoan MCU requires the single-transmembrane protein EMRE. Dictyostelium discoideum (Dd), however, developed a simplified uniporter for which the pore-forming MCU (DdMCU) alone is necessary and sufficient for calcium influx. Here, we report a crystal structure of the N-terminal domain (NTD) of DdMCU at 1.7 A resolution. The DdMCU-NTD contains four helices and two strands arranged in a fold that is completely different from the known structures of other MCU-NTD homologues. Biochemical and biophysical analyses of DdMCU-NTD in solution indicated that the domain exists as high-order oligomers. Mutagenesis showed that the acidic residues Asp60, Glu72, and Glu74, which appeared to mediate the interface II, as observed in the crystal structure, participated in the self-assembly of DdMCU-NTD. Intriguingly, the oligomeric complex was disrupted in the presence of calcium. We propose that the calcium-triggered dissociation of NTD regulates the channel activity of DdMCU by a yet unknown mechanism. | ||
+ | |||
+ | Structural Characterization of the N-Terminal Domain of the Dictyostelium discoideum Mitochondrial Calcium Uniporter.,Yuan Y, Cao C, Wen M, Li M, Dong Y, Wu L, Wu J, Cui T, Li D, Chou JJ, OuYang B ACS Omega. 2020 Mar 20;5(12):6452-6460. doi: 10.1021/acsomega.9b04045., eCollection 2020 Mar 31. PMID:32258880<ref>PMID:32258880</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 5z2h" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Dicdi]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Bo, O]] | [[Category: Bo, O]] | ||
[[Category: Chou, J J]] | [[Category: Chou, J J]] |
Revision as of 21:13, 28 October 2020
Structure of Dictyostelium discoideum mitochondrial calcium uniporter N-terminal domain(DdMCU-NTD)
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Categories: Dicdi | Large Structures | Bo, O | Chou, J J | Li, D | Wen, M | Yuan, Y | Membrane protein