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7bt7

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Current revision (10:49, 27 March 2024) (edit) (undo)
 
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<StructureSection load='7bt7' size='340' side='right'caption='[[7bt7]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
<StructureSection load='7bt7' size='340' side='right'caption='[[7bt7]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[7bt7]] is a 5 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=7BT7 FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6m5g|6m5g]]</td></tr>
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<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>
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<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>
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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=7bt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bt7 OCA], [https://pdbe.org/7bt7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bt7 RCSB], [https://www.ebi.ac.uk/pdbsum/7bt7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bt7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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.
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[https://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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 7bt7" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Actin 3D structures|Actin 3D structures]]
*[[Actin 3D structures|Actin 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Kumari, A]]
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[[Category: Kumari A]]
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[[Category: Ragunath, V K]]
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[[Category: Ragunath VK]]
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[[Category: Sirajuddin, M]]
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[[Category: Sirajuddin M]]
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[[Category: Adp-f-actin]]
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[[Category: Contractile protein]]
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[[Category: F-actin]]
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Current revision

F-actin-ADP complex structure

PDB ID 7bt7

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