6agj - Revision history

OCA at 10:31, 27 March 2024

OCA — Wed, 27 Mar 2024 10:31:42 GMT

←Older revision		Revision as of 10:31, 27 March 2024
Line 3:		Line 3:
	<StructureSection load='6agj' size='340' side='right'caption='[[6agj]], [[Resolution\|resolution]] 3.00Å' scene=''>		<StructureSection load='6agj' size='340' side='right'caption='[[6agj]], [[Resolution\|resolution]] 3.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6agj]] 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=6AGJ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=6AGJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6agj]] is a 2 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=6AGJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AGJ FirstGlance]. <br>
-	</td></tr><tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat">~~MICU3~~, ~~EFHA2 (~~[~~http://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=9606 HUMAN])~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.999Å</td></tr>
-	<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=6agj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6agj OCA], [~~http~~://pdbe.org/6agj PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6agj RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6agj PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6agj ProSAT]</span></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=6agj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6agj OCA], [https://pdbe.org/6agj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6agj RCSB], [https://www.ebi.ac.uk/pdbsum/6agj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6agj ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/MICU3_HUMAN MICU3_HUMAN]] May play a role in mitochondrial calcium uptake.	+	[https://www.uniprot.org/uniprot/MICU3_HUMAN MICU3_HUMAN] May play a role in mitochondrial calcium uptake.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The mitochondrial Ca(2+) uniporter complex (MCUC) is responsible for Ca(2+) influx into the mitochondrial matrix, playing critical roles in various mitochondrial functions. Eukaryotic MCUC consists of multiple subunits, and its Ca(2+) influx activity is controlled by regulatory subunits, including mitochondrial Ca(2+) uptake 1 (MICU1) and its paralogs (MICU2 and MICU3). However, the underlying mechanism remains unclear. Here, we determined multiple crystal structures of MICU2 and MICU3 from Homo sapiens. Our data demonstrate that distinct MICU protein N-domains determine the specific type of MICU dimers that perform the opposing roles in mitochondrial Ca(2+) uptake at low cytosolic Ca(2+) levels. In contrast, at high cytosolic Ca(2+) levels, all MICU proteins undergo dimer rearrangement induced by Ca(2+) binding, which releases the suppression of the MCUC pore-forming subunit and promotes the influx of large amounts of Ca(2+). Altogether, our results elucidate the delicate mechanism of mitochondrial Ca(2+) uptake regulation by MICU proteins.	+
-		+
-	Dimerization of MICU Proteins Controls Ca(2+) Influx through the Mitochondrial Ca(2+) Uniporter.,Xing Y, Wang M, Wang J, Nie Z, Wu G, Yang X, Shen Y Cell Rep. 2019 Jan 29;26(5):1203-1212.e4. doi: 10.1016/j.celrep.2019.01.022. PMID:30699349<ref>PMID:30699349</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 6agj" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
	*[[Calcium uptake protein 3D structures\|Calcium uptake protein 3D structures]]		*[[Calcium uptake protein 3D structures\|Calcium uptake protein 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Xue, Y]]	+	[[Category: Xue Y]]
-	[[Category: Yangfei, X]]	+	[[Category: Yangfei X]]
-	[[Category: Yuequan, S]]	+	[[Category: Yuequan S]]
-	~~[[Category: Calcium]]~~	+
-	~~[[Category: Metal binding protein]]~~	+
-	~~[[Category: Mitochondrial~~]]	+

OCA at 17:16, 14 August 2019

OCA — Wed, 14 Aug 2019 17:16:36 GMT

←Older revision		Revision as of 17:16, 14 August 2019
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6agj is ~~ON HOLD until Paper~~ Publication	+	==Crystal Structure of EFHA2 in Apo State==
		+	<StructureSection load='6agj' size='340' side='right'caption='[[6agj]], [[Resolution\|resolution]] 3.00Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[6agj]] 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=6AGJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AGJ FirstGlance]. <br>
		+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">MICU3, EFHA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<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=6agj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6agj OCA], [http://pdbe.org/6agj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6agj RCSB], [http://www.ebi.ac.uk/pdbsum/6agj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6agj ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/MICU3_HUMAN MICU3_HUMAN]] May play a role in mitochondrial calcium uptake.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The mitochondrial Ca(2+) uniporter complex (MCUC) is responsible for Ca(2+) influx into the mitochondrial matrix, playing critical roles in various mitochondrial functions. Eukaryotic MCUC consists of multiple subunits, and its Ca(2+) influx activity is controlled by regulatory subunits, including mitochondrial Ca(2+) uptake 1 (MICU1) and its paralogs (MICU2 and MICU3). However, the underlying mechanism remains unclear. Here, we determined multiple crystal structures of MICU2 and MICU3 from Homo sapiens. Our data demonstrate that distinct MICU protein N-domains determine the specific type of MICU dimers that perform the opposing roles in mitochondrial Ca(2+) uptake at low cytosolic Ca(2+) levels. In contrast, at high cytosolic Ca(2+) levels, all MICU proteins undergo dimer rearrangement induced by Ca(2+) binding, which releases the suppression of the MCUC pore-forming subunit and promotes the influx of large amounts of Ca(2+). Altogether, our results elucidate the delicate mechanism of mitochondrial Ca(2+) uptake regulation by MICU proteins.

-	~~Authors: Yangfei, X~~., ~~Xue,~~ Y., ~~Yuequan~~, S.	+	Dimerization of MICU Proteins Controls Ca(2+) Influx through the Mitochondrial Ca(2+) Uniporter.,Xing Y, Wang M, Wang J, Nie Z, Wu G, Yang X, Shen Y Cell Rep. 2019 Jan 29;26(5):1203-1212.e4. doi: 10.1016/j.celrep.2019.01.022. PMID:30699349<ref>PMID:30699349</ref>

-	~~Description: Crystal Structure~~ of ~~EFHA2 in Apo State~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[~~Category: Unreleased Structures~~]]	+	</div>
-	[[Category: ~~Yuequan, S~~]]	+	<div class="pdbe-citations 6agj" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Yangfei, X~~]]	+
		+	==See Also==
		+	*[[Calcium uptake protein 3D structures\|Calcium uptake protein 3D structures]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Xue, Y]]		[[Category: Xue, Y]]
		+	[[Category: Yangfei, X]]
		+	[[Category: Yuequan, S]]
		+	[[Category: Calcium]]
		+	[[Category: Metal binding protein]]
		+	[[Category: Mitochondrial]]

OCA at 06:08, 17 October 2018

OCA — Wed, 17 Oct 2018 06:08:03 GMT

←Older revision		Revision as of 06:08, 17 October 2018
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6agj is ON HOLD	+	The entry 6agj is ON HOLD until Paper Publication

	Authors: Yangfei, X., Xue, Y., Yuequan, S.		Authors: Yangfei, X., Xue, Y., Yuequan, S.

OCA: Protected "6agj" [edit=sysop:move=sysop]

OCA — Wed, 22 Aug 2018 04:34:23 GMT

Protected "6agj" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:34, 22 August 2018

OCA: New page: '''Unreleased structure''' The entry 6agj is ON HOLD Authors: Yangfei, X., Xue, Y., Yuequan, S. Description: Crystal Structure of EFHA2 in Apo State Category: Unreleased Structures...

OCA — Wed, 22 Aug 2018 04:34:22 GMT

New page: '''Unreleased structure''' The entry 6agj is ON HOLD Authors: Yangfei, X., Xue, Y., Yuequan, S. Description: Crystal Structure of EFHA2 in Apo State Category: Unreleased Structures...

New page

'''Unreleased structure'''

The entry 6agj is ON HOLD

Authors: Yangfei, X., Xue, Y., Yuequan, S.

Description: Crystal Structure of EFHA2 in Apo State
[[Category: Unreleased Structures]]
[[Category: Yuequan, S]]
[[Category: Yangfei, X]]
[[Category: Xue, Y]]