8dmy: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 8dmy is ~~ON HOLD until Paper~~ Publication

==Cryo-EM structure of cardiac muscle alpha-actin==

== Structural highlights ==

<table><tr><td colspan='2'>[[8dmy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DMY 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>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8dmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dmy OCA], [https://pdbe.org/8dmy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dmy RCSB], [https://www.ebi.ac.uk/pdbsum/8dmy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dmy ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/ACTC_BOVIN ACTC_BOVIN] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

== Publication Abstract from PubMed ==

Actin isoforms organize into distinct networks that are essential for the normal function of eukaryotic cells. Despite a high level of sequence and structure conservation, subtle differences in their design principles determine the interaction with myosin motors and actin-binding proteins. Therefore, identifying how the structure of actin isoforms relates to function is important for our understanding of normal cytoskeletal physiology. Here, we report the high-resolution structures of filamentous skeletal muscle alpha-actin (3.37 A), cardiac muscle alpha-actin (3.07 A), ss-actin (2.99 A), and gamma-actin (3.38 A) in the Mg(2+).ADP state with their native post-translational modifications. The structures revealed isoform-specific conformations of the N-terminus that shift closer to the filament surface upon myosin binding, thereby establishing isoform-specific interfaces. Collectively, the structures of single-isotype, post-translationally modified bare skeletal muscle alpha-actin, cardiac muscle alpha-actin, ss-actin, and gamma-actin reveal general principles, similarities, and differences between isoforms. They complement the repertoire of known actin structures and allow for a comprehensive understanding of in vitro and in vivo functions of actin isoforms.

~~Authors:~~ Arora, A~~.S., Huang~~, ~~H.L.~~, Heissler, ~~S.M.~~, Chinthalapudi, K.

Structural insights into actin isoforms.,Arora AS, Huang HL, Singh R, Narui Y, Suchenko A, Hatano T, Heissler SM, Balasubramanian MK, Chinthalapudi K Elife. 2023 Feb 15;12:e82015. doi: 10.7554/eLife.82015. PMID:36790143<ref>PMID:36790143</ref>

~~Description: Cryo~~-~~EM structure of cardiac muscle alpha~~-~~actin~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased Structures~~]]

</div>

[[Category: ~~Heissler, S.M~~]]

[[Category: ~~Huang, H.L~~]]

== References ==

[[Category: Chinthalapudi, K]]

[[Category: ~~Arora, A.S~~]]

__TOC__

</StructureSection>

[[Category: Bos taurus]]

[[Category: Large Structures]]

[[Category: Arora AS]]

[[Category: Chinthalapudi K]]

[[Category: Heissler SM]]

[[Category: Huang HL]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8dmy is ON HOLD  until Paper Publication
+==Cryo-EM structure of cardiac muscle alpha-actin==
+<StructureSection load='8dmy' size='340' side='right'caption='[[8dmy]], [[Resolution|resolution]] 3.07&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8dmy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DMY 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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8dmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dmy OCA], [https://pdbe.org/8dmy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dmy RCSB], [https://www.ebi.ac.uk/pdbsum/8dmy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dmy ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ACTC_BOVIN ACTC_BOVIN] 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 ==
+Actin isoforms organize into distinct networks that are essential for the normal function of eukaryotic cells. Despite a high level of sequence and structure conservation, subtle differences in their design principles determine the interaction with myosin motors and actin-binding proteins. Therefore, identifying how the structure of actin isoforms relates to function is important for our understanding of normal cytoskeletal physiology. Here, we report the high-resolution structures of filamentous skeletal muscle alpha-actin (3.37 A), cardiac muscle alpha-actin (3.07 A), ss-actin (2.99 A), and gamma-actin (3.38 A) in the Mg(2+).ADP state with their native post-translational modifications. The structures revealed isoform-specific conformations of the N-terminus that shift closer to the filament surface upon myosin binding, thereby establishing isoform-specific interfaces. Collectively, the structures of single-isotype, post-translationally modified bare skeletal muscle alpha-actin, cardiac muscle alpha-actin, ss-actin, and gamma-actin reveal general principles, similarities, and differences between isoforms. They complement the repertoire of known actin structures and allow for a comprehensive understanding of in vitro and in vivo functions of actin isoforms.
-Authors: Arora, A.S., Huang, H.L., Heissler, S.M., Chinthalapudi, K.
+Structural insights into actin isoforms.,Arora AS, Huang HL, Singh R, Narui Y, Suchenko A, Hatano T, Heissler SM, Balasubramanian MK, Chinthalapudi K Elife. 2023 Feb 15;12:e82015. doi: 10.7554/eLife.82015. PMID:36790143<ref>PMID:36790143</ref>
-Description: Cryo-EM structure of cardiac muscle alpha-actin
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Heissler, S.M]]
+<div class="pdbe-citations 8dmy" style="background-color:#fffaf0;"></div>
-[[Category: Huang, H.L]]
+== References ==
-[[Category: Chinthalapudi, K]]
+<references/>
-[[Category: Arora, A.S]]
+__TOC__
+</StructureSection>
+[[Category: Bos taurus]]
+[[Category: Large Structures]]
+[[Category: Arora AS]]
+[[Category: Chinthalapudi K]]
+[[Category: Heissler SM]]
+[[Category: Huang HL]]