7rb8 - Revision history

OCA at 08:29, 4 March 2026

2026-03-04T08:29:13Z

← Older revision		Revision as of 08:29, 4 March 2026
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[7rb8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RB8 FirstGlance]. <br>		<table><tr><td colspan='2'>[[7rb8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RB8 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution\|Resolution]] 3.63Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7rb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rb8 OCA], [https://pdbe.org/7rb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rb8 RCSB], [https://www.ebi.ac.uk/pdbsum/7rb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rb8 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=7rb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rb8 OCA], [https://pdbe.org/7rb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rb8 RCSB], [https://www.ebi.ac.uk/pdbsum/7rb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rb8 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/ACTS_CHICK ACTS_CHICK]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.		[https://www.uniprot.org/uniprot/ACTS_CHICK ACTS_CHICK] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	The motor protein myosin-15 is necessary for the development and maintenance of mechanosensory stereocilia, and mutations in myosin-15 cause hereditary deafness. In addition to transporting actin regulatory machinery to stereocilia tips, myosin-15 directly nucleates actin filament ("F-actin") assembly, which is disrupted by a progressive hearing loss mutation (p.D1647G, "jordan"). Here, we present cryo-electron microscopy structures of myosin-15 bound to F-actin, providing a framework for interpreting the impacts of deafness mutations on motor activity and actin nucleation. Rigor myosin-15 evokes conformational changes in F-actin yet maintains flexibility in actin's D-loop, which mediates inter-subunit contacts, while the jordan mutant locks the D-loop in a single conformation. Adenosine diphosphate-bound myosin-15 also locks the D-loop, which correspondingly blunts actin-polymerization stimulation. We propose myosin-15 enhances polymerization by bridging actin protomers, regulating nucleation efficiency by modulating actin's structural plasticity in a myosin nucleotide state-dependent manner. This tunable regulation of actin polymerization could be harnessed to precisely control stereocilium height.

	Structural basis for tunable control of actin dynamics by myosin-15 in mechanosensory stereocilia.,Gong R, Jiang F, Moreland ZG, Reynolds MJ, de Los Reyes SE, Gurel P, Shams A, Heidings JB, Bowl MR, Bird JE, Alushin GM Sci Adv. 2022 Jul 22;8(29):eabl4733. doi: 10.1126/sciadv.abl4733. Epub 2022 Jul, 20. PMID:35857845<ref>PMID:35857845</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 7rb8" style="background-color:#fffaf0;"></div>~~

	==See Also==		==See Also==
	*[[Actin 3D structures\|Actin 3D structures]]		*[[Actin 3D structures\|Actin 3D structures]]
	*[[Myosin 3D Structures\|Myosin 3D Structures]]		*[[Myosin 3D Structures\|Myosin 3D Structures]]
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 03:51, 8 September 2022

2022-09-08T03:51:45Z

← Older revision		Revision as of 03:51, 8 September 2022
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	====		==cryo-EM structure of the ADP state wild type myosin-15-F-actin complex==
	<StructureSection load='7rb8' size='340' side='right'caption='[[7rb8]]' scene=''>		<StructureSection load='7rb8' size='340' side='right'caption='[[7rb8]], [[Resolution\|resolution]] 3.63Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>		<table><tr><td colspan='2'>[[7rb8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RB8 FirstGlance]. <br>
	</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=7rb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rb8 OCA], [https://pdbe.org/7rb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rb8 RCSB], [https://www.ebi.ac.uk/pdbsum/7rb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rb8 ProSAT]</span></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7rb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rb8 OCA], [https://pdbe.org/7rb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rb8 RCSB], [https://www.ebi.ac.uk/pdbsum/7rb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rb8 ProSAT]</span></td></tr>
	</table>		</table>
			== Function ==
			[[https://www.uniprot.org/uniprot/ACTS_CHICK ACTS_CHICK]] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The motor protein myosin-15 is necessary for the development and maintenance of mechanosensory stereocilia, and mutations in myosin-15 cause hereditary deafness. In addition to transporting actin regulatory machinery to stereocilia tips, myosin-15 directly nucleates actin filament ("F-actin") assembly, which is disrupted by a progressive hearing loss mutation (p.D1647G, "jordan"). Here, we present cryo-electron microscopy structures of myosin-15 bound to F-actin, providing a framework for interpreting the impacts of deafness mutations on motor activity and actin nucleation. Rigor myosin-15 evokes conformational changes in F-actin yet maintains flexibility in actin's D-loop, which mediates inter-subunit contacts, while the jordan mutant locks the D-loop in a single conformation. Adenosine diphosphate-bound myosin-15 also locks the D-loop, which correspondingly blunts actin-polymerization stimulation. We propose myosin-15 enhances polymerization by bridging actin protomers, regulating nucleation efficiency by modulating actin's structural plasticity in a myosin nucleotide state-dependent manner. This tunable regulation of actin polymerization could be harnessed to precisely control stereocilium height.

			Structural basis for tunable control of actin dynamics by myosin-15 in mechanosensory stereocilia.,Gong R, Jiang F, Moreland ZG, Reynolds MJ, de Los Reyes SE, Gurel P, Shams A, Heidings JB, Bowl MR, Bird JE, Alushin GM Sci Adv. 2022 Jul 22;8(29):eabl4733. doi: 10.1126/sciadv.abl4733. Epub 2022 Jul, 20. PMID:35857845<ref>PMID:35857845</ref>

			From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
			<div class="pdbe-citations 7rb8" style="background-color:#fffaf0;"></div>

			==See Also==
			*[[Actin 3D structures\|Actin 3D structures]]
			*[[Myosin 3D Structures\|Myosin 3D Structures]]
			== References ==
			<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Gallus gallus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: ~~Z-disk~~]]		[[Category: Mus musculus]]
			[[Category: Alushin GM]]
			[[Category: Gong R]]
			[[Category: Gurel P]]
			[[Category: Reynolds MJ]]

OCA at 10:36, 28 July 2021

2021-07-28T10:36:27Z

← Older revision		Revision as of 10:36, 28 July 2021
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	~~'''Unreleased structure'''~~

	~~The entry~~ 7rb8 is ~~ON HOLD~~		====
			<StructureSection load='7rb8' size='340' side='right'caption='[[7rb8]]' scene=''>
	~~Authors:~~		== Structural highlights ==
			<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br>
	~~Description~~:		</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=7rb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rb8 OCA], [https://pdbe.org/7rb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rb8 RCSB], [https://www.ebi.ac.uk/pdbsum/7rb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rb8 ProSAT]</span></td></tr>
	[[Category: ~~Unreleased Structures~~]]		</table>
			__TOC__
			</StructureSection>
			[[Category: Large Structures]]
			[[Category: Z-disk]]

OCA: Protected "7rb8" [edit=sysop:move=sysop]

2021-07-14T08:55:38Z

Protected "7rb8" [edit=sysop:move=sysop]

← Older revision	Revision as of 08:55, 14 July 2021
(No difference)

OCA: New page: '''Unreleased structure''' The entry 7rb8 is ON HOLD Authors: Description: Category: Unreleased Structures

2021-07-14T08:55:37Z

New page: '''Unreleased structure''' The entry 7rb8 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 7rb8 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]