View source for 7sog


==Thermostable actophorin==
<StructureSection load='7sog' size='340' side='right'caption='[[7sog]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7sog]] is a 2 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=7SOG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SOG 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]] 1.74&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=7sog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7sog OCA], [https://pdbe.org/7sog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7sog RCSB], [https://www.ebi.ac.uk/pdbsum/7sog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7sog 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, which was recently tested for crystallization under microgravity on the International Space Station, was subjected to mutagenesis to identify a construct with improved biophysical properties that were expected to improve the extent of diffraction. First, 20 mutations, including one C-terminal deletion of three residues, were introduced individually into actophorin, resulting in modest increases in thermal stability of between +0.5 degrees C and +2.2 degrees C. All but two of the stabilizing mutants increased both the rates of severing F-actin filaments and of spontaneous polymerization of pyrenyl G-actin in vitro. When the individual mutations were combined into a single actophorin variant, Acto-2, the overall thermal stability was 22 degrees C higher than that of wild-type actophorin. When an inactivating S2P mutation in Acto-2 was restored, Acto-2/P2S was more stable by 20 degrees C but was notably more active than the wild-type protein. The inactivating S2P mutation reaffirms the importance that Ser2 plays in the F-actin-severing reaction. The crystal structure of Acto-2 was solved to 1.7 A resolution in a monoclinic space group, a first for actophorin. Surprisingly, despite the increase in thermal stability, the extended beta-turn region, which is intimately involved in interactions with F-actin, is disordered in one copy of Acto-2 in the asymmetric unit. These observations emphasize the complex interplay among protein thermal stability, function and dynamics.

Structure and activity of a thermally stable mutant of Acanthamoeba actophorin.,Quirk S, Lieberman RL Acta Crystallogr F Struct Biol Commun. 2022 Apr 1;78(Pt 4):150-160. doi:, 10.1107/S2053230X22002448. Epub 2022 Mar 28. PMID:35400667<ref>PMID:35400667</ref>

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