6iih

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<StructureSection load='6iih' size='340' side='right'caption='[[6iih]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
<StructureSection load='6iih' size='340' side='right'caption='[[6iih]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6iih]] is a 2 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=6IIH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IIH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6iih]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IIH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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]] 1.958&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MICU2, EFHA1 ([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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></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=6iih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iih OCA], [https://pdbe.org/6iih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iih RCSB], [https://www.ebi.ac.uk/pdbsum/6iih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iih 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=6iih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iih OCA], [http://pdbe.org/6iih PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6iih RCSB], [http://www.ebi.ac.uk/pdbsum/6iih PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6iih ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4]] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref>
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[https://www.uniprot.org/uniprot/MICU2_HUMAN MICU2_HUMAN] Key regulator of mitochondrial calcium uniporter (MCU) required to limit calcium uptake by MCU when cytoplasmic calcium is low (PubMed:24503055, PubMed:24560927, PubMed:26903221). MICU1 and MICU2 form a disulfide-linked heterodimer that stimulate and inhibit MCU activity, depending on the concentration of calcium (PubMed:24560927). MICU2 acts as a gatekeeper of MCU that senses calcium level via its EF-hand domains: prevents channel opening at resting calcium, avoiding energy dissipation and cell-death triggering (PubMed:24560927).<ref>PMID:24503055</ref> <ref>PMID:24560927</ref> <ref>PMID:26387864</ref> <ref>PMID:26903221</ref> [https://www.uniprot.org/uniprot/ENLYS_BPT4 ENLYS_BPT4] Endolysin with lysozyme activity that degrades host peptidoglycans and participates with the holin and spanin proteins in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles. Once the holin has permeabilized the host cell membrane, the endolysin can reach the periplasm and break down the peptidoglycan layer.<ref>PMID:22389108</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The mitochondrial calcium uniporter (MCU) complex mediates the uptake of Ca(2+) into mitochondria. Its activity is regulated by a heterodimer of MICU1 and MICU2, two EF-hand-containing proteins that act as the main gatekeeper of the uniporter. Herein we report the crystal structure of human MICU2 at 1.96 A resolution. Our structure reveals a dimeric architecture of MICU2, in which each monomer adopts the canonical two-lobe structure with a pair of EF-hands in each lobe. Both Ca(2+) -bound and Ca(2+) -free EF-hands are observed in our structure. Moreover, we characterize the interaction sites within the MICU2 homodimer, as well as the MICU1-MICU2 heterodimer in both Ca(2+) -free and Ca(2+) -bound conditions. Glu242 in MICU1 and Arg352 in MICU2 are crucial for apo heterodimer formation, while Phe383 in MICU1 and Glu196 in MICU2 significantly contribute to the interaction in the Ca(2+) -bound state. Based on our structural and biochemical analyses, we propose a model for MICU1-MICU2 heterodimer formation and its conformational transition from apo to a more compact Ca(2+) -bound state, which expands our understanding of this co-regulatory mechanism critical for MCU's mitochondrial calcium uptake function.
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The crystal structure of MICU2 provides insight into Ca(2+) binding and MICU1-MICU2 heterodimer formation.,Wu W, Shen Q, Lei Z, Qiu Z, Li D, Pei H, Zheng J, Jia Z EMBO Rep. 2019 Sep;20(9):e47488. doi: 10.15252/embr.201847488. Epub 2019 Aug 9. PMID:31397067<ref>PMID:31397067</ref>
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==See Also==
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*[[Calcium uptake protein 3D structures|Calcium uptake protein 3D structures]]
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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 6iih" 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: Escherichia virus T4]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Lysozyme]]
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[[Category: Jia Z]]
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[[Category: Jia, Z]]
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[[Category: Shen Q]]
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[[Category: Shen, Q]]
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[[Category: Wu W]]
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[[Category: Wu, W]]
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[[Category: Zheng J]]
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[[Category: Zheng, J]]
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[[Category: Calcium binding protein]]
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[[Category: Ef-hand]]
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[[Category: Metal binding protein]]
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[[Category: Mitochondrial]]
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[[Category: T4l fusion protein]]
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Current revision

crystal structure of mitochondrial calcium uptake 2(MICU2)

PDB ID 6iih

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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