6k2g: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
'''Unreleased structure'''


The entry 6k2g is ON HOLD  until Paper Publication
==Structure of FraE in the monomer state==
<StructureSection load='6k2g' size='340' side='right'caption='[[6k2g]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6k2g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K2G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6K2G FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6k2g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k2g OCA], [http://pdbe.org/6k2g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k2g RCSB], [http://www.ebi.ac.uk/pdbsum/6k2g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k2g ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Random mutations and selective pressure drive protein adaptation to the changing demands of the environment. As a consequence, nature favors the evolution of protein diversity. A group of proteins subject to exceptional environmental stress and known for their widespread diversity are the pore-forming hemolytic proteins from sea anemones, known as actinoporins. In this study, we identified and isolated new isoforms of actinoporins from the sea anemone Actinia fragacea (fragaceatoxins). We characterized their hemolytic activity, examined their stability and structure, and performed a comparative analysis of their primary sequence. Sequence alignment reveals that most of the variability among actinoporins is associated with non-functional residues. The differences in the thermal behavior among fragaceatoxins suggest that these variability sites contribute to changes in protein stability. In addition, the protein-protein interaction region showed a very high degree of identity (92%) within fragaceatoxins, but only 25% among all actinoporins examined, suggesting some degree of specificity at the species level. Our findings support the mechanism of evolutionary adaptation in actinoporins and reflect common pathways conducive to protein variability.


Authors:  
The Isolation of New Pore-Forming Toxins from the Sea Anemone Actinia fragacea Provides Insights into the Mechanisms of Actinoporin Evolution.,Morante K, Bellomio A, Viguera AR, Gonzalez-Manas JM, Tsumoto K, Caaveiro JMM Toxins (Basel). 2019 Jul 10;11(7). pii: toxins11070401. doi:, 10.3390/toxins11070401. PMID:31295915<ref>PMID:31295915</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6k2g" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Caaveiro, J M.M]]
[[Category: Morante, K]]
[[Category: Tsumoto, K]]
[[Category: Actinoporin]]
[[Category: Hemolysis]]
[[Category: Pore forming protein]]
[[Category: Protein evolution]]
[[Category: Toxin]]
Retrieved from "https://proteopedia.org/6k2g"