8rtt: Difference between revisions

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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=8rtt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rtt OCA], [https://pdbe.org/8rtt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rtt RCSB], [https://www.ebi.ac.uk/pdbsum/8rtt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rtt 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=8rtt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8rtt OCA], [https://pdbe.org/8rtt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8rtt RCSB], [https://www.ebi.ac.uk/pdbsum/8rtt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8rtt ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/ACTB_HUMAN ACTB_HUMAN] Defects in ACTB are a cause of dystonia juvenile-onset (DYTJ) [MIM:[https://omim.org/entry/607371 607371]. DYTJ is a form of dystonia with juvenile onset. Dystonia is defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. DYTJ patients manifest progressive, generalized, dopa-unresponsive dystonia, developmental malformations and sensory hearing loss.<ref>PMID:16685646</ref>  Defects in ACTB are the cause of Baraitser-Winter syndrome type 1 (BRWS1) [MIM:[https://omim.org/entry/243310 243310]. A rare developmental disorder characterized by the combination of congenital ptosis, high-arched eyebrows, hypertelorism, ocular colobomata, and a brain malformation consisting of anterior-predominant lissencephaly. Other typical features include postnatal short stature and microcephaly, intellectual disability, seizures, and hearing loss.<ref>PMID:22366783</ref>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/ACTB_HUMAN ACTB_HUMAN] 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/CDC12_SCHPO CDC12_SCHPO] Plays a role in the cell cycle. Involved in cytokinesis. Component of the cell division ring. In the absence of profilin, caps the barbed end of actin filaments, thus preventing subunit addition and dissociation. In the presence of profilin, nucleates actin filaments that grow rapidly from their barbed ends.<ref>PMID:12796476</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Formins control the assembly of actin filaments (F-actin) that drive cell morphogenesis and motility in eukaryotes. However, their molecular interaction with F-actin and their mechanism of action remain unclear. In this work, we present high-resolution cryo-electron microscopy structures of F-actin barbed ends bound by three distinct formins, revealing a common asymmetric formin conformation imposed by the filament. Formation of new intersubunit contacts during actin polymerization sterically displaces formin and triggers its translocation. This "undock-and-lock" mechanism explains how actin-filament growth is coordinated with formin movement. Filament elongation speeds are controlled by the positioning and stability of actin-formin interfaces, which distinguish fast and slow formins. Furthermore, we provide a structure of the actin-formin-profilin ring complex, which resolves how profilin is rapidly released from the barbed end during filament elongation.
 
Molecular mechanism of actin filament elongation by formins.,Oosterheert W, Boiero Sanders M, Funk J, Prumbaum D, Raunser S, Bieling P Science. 2024 Apr 12;384(6692):eadn9560. doi: 10.1126/science.adn9560. Epub 2024 , Apr 12. PMID:38603491<ref>PMID:38603491</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8rtt" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Latest revision as of 08:59, 5 June 2024

Structure of the formin Cdc12 bound to the barbed end of phalloidin-stabilized F-actin.Structure of the formin Cdc12 bound to the barbed end of phalloidin-stabilized F-actin.

Structural highlights

8rtt is a 9 chain structure with sequence from Amanita phalloides, Homo sapiens and Schizosaccharomyces pombe. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.56Å
Ligands:, , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CDC12_SCHPO Plays a role in the cell cycle. Involved in cytokinesis. Component of the cell division ring. In the absence of profilin, caps the barbed end of actin filaments, thus preventing subunit addition and dissociation. In the presence of profilin, nucleates actin filaments that grow rapidly from their barbed ends.[1]

Publication Abstract from PubMed

Formins control the assembly of actin filaments (F-actin) that drive cell morphogenesis and motility in eukaryotes. However, their molecular interaction with F-actin and their mechanism of action remain unclear. In this work, we present high-resolution cryo-electron microscopy structures of F-actin barbed ends bound by three distinct formins, revealing a common asymmetric formin conformation imposed by the filament. Formation of new intersubunit contacts during actin polymerization sterically displaces formin and triggers its translocation. This "undock-and-lock" mechanism explains how actin-filament growth is coordinated with formin movement. Filament elongation speeds are controlled by the positioning and stability of actin-formin interfaces, which distinguish fast and slow formins. Furthermore, we provide a structure of the actin-formin-profilin ring complex, which resolves how profilin is rapidly released from the barbed end during filament elongation.

Molecular mechanism of actin filament elongation by formins.,Oosterheert W, Boiero Sanders M, Funk J, Prumbaum D, Raunser S, Bieling P Science. 2024 Apr 12;384(6692):eadn9560. doi: 10.1126/science.adn9560. Epub 2024 , Apr 12. PMID:38603491[2]

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

References

  1. ↑ Kovar DR, Kuhn JR, Tichy AL, Pollard TD. The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin. J Cell Biol. 2003 Jun 9;161(5):875-87. PMID:12796476 doi:10.1083/jcb.200211078
  2. ↑ Oosterheert W, Boiero Sanders M, Funk J, Prumbaum D, Raunser S, Bieling P. Molecular mechanism of actin filament elongation by formins. Science. 2024 Apr 12;384(6692):eadn9560. PMID:38603491 doi:10.1126/science.adn9560

8rtt, resolution 3.56Å

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