1sjj

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Current revision (08:31, 14 February 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1sjj]] is a 2 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=1SJJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SJJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[1sjj]] is a 2 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=1SJJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SJJ FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1hci|1hci]], [[1aoa|1aoa]], [[1dxx|1dxx]], [[1qag|1qag]], [[1cfd|1cfd]]</div></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 crystallography, [[Resolution|Resolution]] 20&#8491;</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=1sjj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sjj OCA], [https://pdbe.org/1sjj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sjj RCSB], [https://www.ebi.ac.uk/pdbsum/1sjj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sjj 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=1sjj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sjj OCA], [https://pdbe.org/1sjj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sjj RCSB], [https://www.ebi.ac.uk/pdbsum/1sjj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sjj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/ACTN1_CHICK ACTN1_CHICK]] F-actin cross-linking protein is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.
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[https://www.uniprot.org/uniprot/ACTN1_CHICK ACTN1_CHICK] F-actin cross-linking protein is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1sjj ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1sjj ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Cryoelectron microscopy was used to obtain a 3-D image at 2.0 nm resolution of 2-D arrays of smooth muscle alpha-actinin. The reconstruction reveals a well-resolved long central domain with 90 degrees of left-handed twist and near 2-fold symmetry. However, the molecular ends which contain the actin binding and calmodulin-like domains, have different structures oriented approximately 90 degrees to each other. Atomic structures for the alpha-actinin domains were built by homology modeling and assembled into an atomic model. Model building suggests that in the 2-D arrays, the two calponin homology domains that comprise the actin-binding domain have a closed conformation at one end and an open conformation at the other end due to domain swapping. The open and closed conformations of the actin-binding domain suggests flexibility that may underlie Ca2+ regulation. The approximately 90 degrees orientation difference at the molecular ends may underlie alpha-actinin's ability to crosslink actin filaments in nearly any orientation.
 
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A 3-D reconstruction of smooth muscle alpha-actinin by CryoEm reveals two different conformations at the actin-binding region.,Liu J, Taylor DW, Taylor KA J Mol Biol. 2004 Apr 16;338(1):115-25. PMID:15050827<ref>PMID:15050827</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 1sjj" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Actinin 3D structures|Actinin 3D structures]]
*[[Actinin 3D structures|Actinin 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: Liu, J]]
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[[Category: Liu J]]
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[[Category: Taylor, D W]]
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[[Category: Taylor DW]]
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[[Category: Taylor, K A]]
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[[Category: Taylor KA]]
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[[Category: 3-helix bundle]]
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[[Category: Actin binding protein]]
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[[Category: Calmodulin-like domain]]
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[[Category: Calponin homology domain]]
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[[Category: Contractile protein]]
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Current revision

Cryo-EM Structure of Chicken Gizzard Smooth Muscle alpha-Actinin

PDB ID 1sjj

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