7bt7: Difference between revisions
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==F-actin-ADP complex structure== | ==F-actin-ADP complex structure== | ||
<StructureSection load='7bt7' size='340' side='right'caption='[[7bt7]]' scene=''> | <StructureSection load='7bt7' size='340' side='right'caption='[[7bt7]], [[Resolution|resolution]] 3.80Å' 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=7BT7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7BT7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7bt7]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BT7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7BT7 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7bt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bt7 OCA], [http://pdbe.org/7bt7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7bt7 RCSB], [http://www.ebi.ac.uk/pdbsum/7bt7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7bt7 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></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6m5g|6m5g]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7bt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bt7 OCA], [http://pdbe.org/7bt7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7bt7 RCSB], [http://www.ebi.ac.uk/pdbsum/7bt7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7bt7 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[http://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 == | |||
Cellular studies of filamentous actin (F-actin) processes commonly utilize fluorescent versions of toxins, peptides, and proteins that bind actin. While the choice of these markers has been largely based on availability and ease, there is a severe dearth of structural data for an informed judgment in employing suitable F-actin markers for a particular requirement. Here, we describe the electron cryomicroscopy structures of phalloidin, lifeAct, and utrophin bound to F-actin, providing a comprehensive high-resolution structural comparison of widely used actin markers and their influence towards F-actin. Our results show that phalloidin binding does not induce specific conformational change and lifeAct specifically recognizes closed D-loop conformation, i.e., ADP-Pi or ADP states of F-actin. The structural models aided designing of minimal utrophin and a shorter lifeAct, which can be utilized as F-actin marker. Together, our study provides a structural perspective, where the binding sites of utrophin and lifeAct overlap with majority of actin-binding proteins and thus offering an invaluable resource for researchers in choosing appropriate actin markers and generating new marker variants. | |||
Structural insights into actin filament recognition by commonly used cellular actin markers.,Kumari A, Kesarwani S, Javoor MG, Vinothkumar KR, Sirajuddin M EMBO J. 2020 Jul 15;39(14):e104006. doi: 10.15252/embj.2019104006. Epub 2020 Jun , 22. PMID:32567727<ref>PMID:32567727</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7bt7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Actin 3D structures|Actin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Gallus gallus]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kumari A]] | [[Category: Kumari, A]] | ||
[[Category: Ragunath | [[Category: Ragunath, V K]] | ||
[[Category: Sirajuddin M]] | [[Category: Sirajuddin, M]] | ||
[[Category: Adp-f-actin]] | |||
[[Category: Contractile protein]] | |||
[[Category: F-actin]] | |||
Revision as of 14:49, 22 July 2020
F-actin-ADP complex structureF-actin-ADP complex structure
Structural highlights
Function[ACTS_CHICK] 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 PubMedCellular studies of filamentous actin (F-actin) processes commonly utilize fluorescent versions of toxins, peptides, and proteins that bind actin. While the choice of these markers has been largely based on availability and ease, there is a severe dearth of structural data for an informed judgment in employing suitable F-actin markers for a particular requirement. Here, we describe the electron cryomicroscopy structures of phalloidin, lifeAct, and utrophin bound to F-actin, providing a comprehensive high-resolution structural comparison of widely used actin markers and their influence towards F-actin. Our results show that phalloidin binding does not induce specific conformational change and lifeAct specifically recognizes closed D-loop conformation, i.e., ADP-Pi or ADP states of F-actin. The structural models aided designing of minimal utrophin and a shorter lifeAct, which can be utilized as F-actin marker. Together, our study provides a structural perspective, where the binding sites of utrophin and lifeAct overlap with majority of actin-binding proteins and thus offering an invaluable resource for researchers in choosing appropriate actin markers and generating new marker variants. Structural insights into actin filament recognition by commonly used cellular actin markers.,Kumari A, Kesarwani S, Javoor MG, Vinothkumar KR, Sirajuddin M EMBO J. 2020 Jul 15;39(14):e104006. doi: 10.15252/embj.2019104006. Epub 2020 Jun , 22. PMID:32567727[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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