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==Cryo-EM structure of F-actin stabilized by cis-optoJASP-8==
==Cryo-EM structure of F-actin stabilized by cis-optoJASP-8==
<StructureSection load='7ahn' size='340' side='right'caption='[[7ahn]]' scene=''>
<StructureSection load='7ahn' size='340' side='right'caption='[[7ahn]], [[Resolution|resolution]] 2.90&Aring;' 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=7AHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AHN FirstGlance]. <br>
<table><tr><td colspan='2'>[[7ahn]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AHN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AHN 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=7ahn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ahn OCA], [https://pdbe.org/7ahn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ahn RCSB], [https://www.ebi.ac.uk/pdbsum/7ahn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ahn 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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=RLZ:~{N}-[4-[(4~{R},7~{R},10~{S},13~{S},15~{E},19~{S})-4-(4-hydroxyphenyl)-7-(1~{H}-indol-3-ylmethyl)-8,13,15,19-tetramethyl-2,6,9,12-tetrakis(oxidanylidene)-1-oxa-5,8,11-triazacyclononadec-15-en-10-yl]butyl]-~{N}-[5-methoxy-2-[(~{Z})-(3,4,5-trimethoxyphenyl)diazenyl]phenyl]butanediamide'>RLZ</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</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=7ahn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ahn OCA], [https://pdbe.org/7ahn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ahn RCSB], [https://www.ebi.ac.uk/pdbsum/7ahn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ahn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT]] 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 is essential for key processes in all eukaryotic cells. Cellpermeable optojasps provide spatiotemporal control of the actin cytoskeleton, confining toxicity and potentially rendering F-actin druggable by photopharmacology. Here, we report cryo electron microscopy (cryo-EM) structures of both isomeric states of one optojasp bound to actin filaments. The high-resolution structures reveal for the first time the pronounced effects of photoswitching a functionalized azobenzene. By characterizing the optojasp binding site and identifying conformational changes within F-actin that depend on the optojasp isomeric state, we refine determinants for the design of functional F-actin photoswitches.
Cryo-EM resolves molecular recognition of an optojasp photoswitch bound to actin filaments in both switch states.,Pospich S, Kullmer F, Nasufovic V, Funk J, Belyy A, Bieling P, Arndt HD, Raunser S Angew Chem Int Ed Engl. 2021 Jan 15. doi: 10.1002/anie.202013193. PMID:33449370<ref>PMID:33449370</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ahn" style="background-color:#fffaf0;"></div>
==See Also==
*[[Actin 3D structures|Actin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pospich S]]
[[Category: Oryctolagus cuniculus]]
[[Category: Raunser S]]
[[Category: Pospich, S]]
[[Category: Raunser, S]]
[[Category: Azobenzene photoswitch]]
[[Category: Cytoskeleton]]
[[Category: Jasplakinolide]]
[[Category: Stabilized-actin filament]]
[[Category: Structural protein]]

Latest revision as of 09:56, 14 April 2021

Cryo-EM structure of F-actin stabilized by cis-optoJASP-8Cryo-EM structure of F-actin stabilized by cis-optoJASP-8

Structural highlights

7ahn is a 5 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
NonStd Res:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ACTS_RABIT] 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 is essential for key processes in all eukaryotic cells. Cellpermeable optojasps provide spatiotemporal control of the actin cytoskeleton, confining toxicity and potentially rendering F-actin druggable by photopharmacology. Here, we report cryo electron microscopy (cryo-EM) structures of both isomeric states of one optojasp bound to actin filaments. The high-resolution structures reveal for the first time the pronounced effects of photoswitching a functionalized azobenzene. By characterizing the optojasp binding site and identifying conformational changes within F-actin that depend on the optojasp isomeric state, we refine determinants for the design of functional F-actin photoswitches.

Cryo-EM resolves molecular recognition of an optojasp photoswitch bound to actin filaments in both switch states.,Pospich S, Kullmer F, Nasufovic V, Funk J, Belyy A, Bieling P, Arndt HD, Raunser S Angew Chem Int Ed Engl. 2021 Jan 15. doi: 10.1002/anie.202013193. PMID:33449370[1]

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

See Also

References

  1. Pospich S, Kullmer F, Nasufovic V, Funk J, Belyy A, Bieling P, Arndt HD, Raunser S. Cryo-EM resolves molecular recognition of an optojasp photoswitch bound to actin filaments in both switch states. Angew Chem Int Ed Engl. 2021 Jan 15. doi: 10.1002/anie.202013193. PMID:33449370 doi:http://dx.doi.org/10.1002/anie.202013193

7ahn, resolution 2.90Å

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