View source for 8fam


==Edited Octopus bimaculoides Synaptotagmin 1 C2A (I248V) at room temperature==
<StructureSection load='8fam' size='340' side='right'caption='[[8fam]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8fam]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Octopus_bimaculoides Octopus bimaculoides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FAM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FAM 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]] 1.95&#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=8fam FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fam OCA], [https://pdbe.org/8fam PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fam RCSB], [https://www.ebi.ac.uk/pdbsum/8fam PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fam ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0L8IHK9_OCTBM A0A0L8IHK9_OCTBM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In poikilotherms, temperature changes challenge the integration of physiological function. Within the complex nervous systems of the behaviorally sophisticated coleoid cephalopods, these problems are substantial. RNA editing by adenosine deamination is a well-positioned mechanism for environmental acclimation. We report that the neural proteome of Octopus bimaculoides undergoes massive reconfigurations via RNA editing following a temperature challenge. Over 13,000 codons are affected, and many alter proteins that are vital for neural processes. For two highly temperature-sensitive examples, recoding tunes protein function. For synaptotagmin, a key component of Ca(2+)-dependent neurotransmitter release, crystal structures and supporting experiments show that editing alters Ca(2+) binding. For kinesin-1, a motor protein driving axonal transport, editing regulates transport velocity down microtubules. Seasonal sampling of wild-caught specimens indicates that temperature-dependent editing occurs in the field as well. These data show that A-to-I editing tunes neurophysiological function in response to temperature in octopus and most likely other coleoids.

Temperature-dependent RNA editing in octopus extensively recodes the neural proteome.,Birk MA, Liscovitch-Brauer N, Dominguez MJ, McNeme S, Yue Y, Hoff JD, Twersky I, Verhey KJ, Sutton RB, Eisenberg E, Rosenthal JJC Cell. 2023 Jun 8;186(12):2544-2555.e13. doi: 10.1016/j.cell.2023.05.004. Epub , 2023 Jun 8. PMID:37295402<ref>PMID:37295402</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8fam" style="background-color:#fffaf0;"></div>

==See Also==
*[[Synaptotagmin 3D structures|Synaptotagmin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Octopus bimaculoides]]
[[Category: Birk MA]]
[[Category: Dominguez MJ]]
[[Category: McNeme S]]
[[Category: Rosenthal JJ]]
[[Category: Sutton RB]]