View source for 7aw8


==Alpha-actinin in Rhodamnia argentea==
<StructureSection load='7aw8' size='340' side='right'caption='[[7aw8]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7aw8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodamnia_argentea Rhodamnia argentea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AW8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AW8 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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=7aw8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7aw8 OCA], [https://pdbe.org/7aw8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7aw8 RCSB], [https://www.ebi.ac.uk/pdbsum/7aw8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7aw8 ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The Australian tree malletwood (Rhodamnia argentea) is unique. The genome of malletwood is the only known plant genome that contains a gene coding for an alpha-actinin-like protein. Several organisms predating the animal-plant bifurcation express an alpha-actinin or alpha-actinin-like protein. Therefore, it appears that plants in general, but not malletwood, have lost the alpha-actinin or alpha-actinin-like gene during evolution. In order to characterize its structure and function, we synthesized the gene and expressed the recombinant R. argentea protein. The results clearly show that this protein has all properties of genuine alpha-actinin. The N-terminal actin-binding domain (ABD), with two calponin homology motifs, is very similar to the ABD of any alpha-actinin. The C-terminal calmodulin-like domain, as well as the intervening rod domain, are also similar to the corresponding regions in other alpha-actinins. The R. argentea alpha-actinin-like protein dimerises in solution and thereby can cross-link actin filaments. Based on these results, we believe the R. argentea protein represents a genuine alpha-actinin, making R. argentea unique in the plant world.

Structural and functional characterization of a plant alpha-actinin.,Persson K, Backman L FEBS Open Bio. 2021 Jun 10. doi: 10.1002/2211-5463.13222. PMID:34110107<ref>PMID:34110107</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 7aw8" style="background-color:#fffaf0;"></div>

==See Also==
*[[Actinin 3D structures|Actinin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodamnia argentea]]
[[Category: Backman L]]
[[Category: Persson K]]