8dnf: Difference between revisions
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The entry | ==Cryo-EM structure of nonmuscle gamma-actin== | ||
<StructureSection load='8dnf' size='340' side='right'caption='[[8dnf]], [[Resolution|resolution]] 3.38Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8dnf]] is a 4 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=8DNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DNF FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <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=8dnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8dnf OCA], [https://pdbe.org/8dnf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8dnf RCSB], [https://www.ebi.ac.uk/pdbsum/8dnf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8dnf ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/ACTG_HUMAN ACTG_HUMAN] Baraitser-Winter syndrome;Autosomal dominant non-syndromic sensorineural deafness type DFNA. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ACTG_HUMAN ACTG_HUMAN] 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8dnf" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Chinthalapudi | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Arora AS]] | |||
[[Category: Chinthalapudi K]] | |||
[[Category: Heissler SM]] | |||
[[Category: Huang HL]] | |||
Latest revision as of 23:31, 12 April 2023
Cryo-EM structure of nonmuscle gamma-actinCryo-EM structure of nonmuscle gamma-actin
Structural highlights
DiseaseACTG_HUMAN Baraitser-Winter syndrome;Autosomal dominant non-syndromic sensorineural deafness type DFNA. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. FunctionACTG_HUMAN 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 PubMedActin 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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