View source for 7rtx


==Actophorin grown in microgravity==
<StructureSection load='7rtx' size='340' side='right'caption='[[7rtx]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7rtx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7RTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7RTX 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]] 1.65&#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=7rtx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7rtx OCA], [https://pdbe.org/7rtx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7rtx RCSB], [https://www.ebi.ac.uk/pdbsum/7rtx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7rtx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACTP_ACACA ACTP_ACACA] Forms a one to one complex with monomeric actin. Can regulate the pool available for polymerization. Severs actin filaments in a dose-dependent manner.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Actophorin, a protein that severs actin filaments isolated from the amoeba Acanthamoeba castellanii, was employed as a test case for crystallization under microgravity. Crystals of purified actophorin were grown under microgravity conditions aboard the International Space Station (ISS) utilizing an interactive crystallization setup between the ISS crew and ground-based experimenters. Crystals grew in conditions similar to those grown on earth. The structure was solved by molecular replacement at a resolution of 1.65 A. Surprisingly, the structure reveals conformational changes in a remote beta-turn region that were previously associated with actophorin phosphorylated at the terminal residue Ser1. Although crystallization under microgravity did not yield a higher resolution than crystals grown under typical laboratory conditions, the conformation of actophorin obtained from solving the structure suggests greater flexibility in the actophorin beta-turn than previously appreciated and may be beneficial for the binding of actophorin to actin filaments.

Improved resolution crystal structure of Acanthamoeba actophorin reveals structural plasticity not induced by microgravity.,Quirk S, Lieberman RL Acta Crystallogr F Struct Biol Commun. 2021 Dec 1;77(Pt 12):452-458. doi:, 10.1107/S2053230X21011419. Epub 2021 Nov 11. PMID:34866600<ref>PMID:34866600</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7rtx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Acanthamoeba castellanii]]
[[Category: Large Structures]]
[[Category: Lieberman RL]]
[[Category: Quirk S]]