4mn0: Difference between revisions
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== | ==Spatial structure of the novel light-sensitive photoprotein berovin from the ctenophore Beroe abyssicola in the Ca2+-loaded apoprotein conformation state== | ||
[[4mn0]] is a 1 chain structure with sequence from [ | <StructureSection load='4mn0' size='340' side='right'caption='[[4mn0]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4mn0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Beroe_abyssicola Beroe abyssicola]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2hpk 2hpk]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MN0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MN0 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4mn0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mn0 OCA], [https://pdbe.org/4mn0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mn0 RCSB], [https://www.ebi.ac.uk/pdbsum/4mn0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mn0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/H8ZZK1_BERAB H8ZZK1_BERAB] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The bright bioluminescence of ctenophores, found in oceans worldwide, is determined by Ca(2+)-regulated photoproteins, functionally identical to and sharing many properties of hydromedusan photoproteins. In contrast, however, the ctenophore photoproteins are extremely sensitive to UV and visible light over the range of their absorption spectrum. The spatial structure of a novel light-sensitive photoprotein from the ctenophore Beroe abyssicola in its apoform bound with three calcium ions is determined at 2.0A. We demonstrate that the apoberovin is a slightly asymmetrical compact globular protein formed by two domains with a cavity in the center, which exactly retains the fold architecture characteristic of hydromedusan photoproteins despite their low amino acid sequence identity. However, the structural alignment of these two photoprotein classes clearly shows that despite the high similarity of shape and geometry of their coelenterazine-binding cavities, their interiors differ drastically. The key residues appearing to be crucial for stabilizing the 2-hydroperoxycoelenterazine and for formation of the emitter in hydromedusan photoproteins, are replaced in berovin by amino acid residues having completely different side chain properties. Evidently, these replacements must be responsible for the distinct properties of ctenophore photoproteins such as sensitivity to light or the fact that the formation of active photoprotein from apophotoprotein, coelenterazine, and oxygen is more effective at alkaline pH. | |||
Spatial structure of the novel light-sensitive photoprotein berovin from the ctenophore Beroe abyssicola in the Ca(2+)-loaded apoprotein conformation state.,Stepanyuk GA, Liu ZJ, Burakova LP, Lee J, Rose J, Vysotski ES, Wang BC Biochim Biophys Acta. 2013 Oct;1834(10):2139-46. doi:, 10.1016/j.bbapap.2013.07.006. Epub 2013 Jul 25. PMID:23891746<ref>PMID:23891746</ref> | |||
<ref | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4mn0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Beroe abyssicola]] | [[Category: Beroe abyssicola]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Lee J]] | ||
[[Category: | [[Category: Liu ZJ]] | ||
[[Category: | [[Category: Rose JP]] | ||
[[Category: Stepanyuk | [[Category: Stepanyuk GA]] | ||
[[Category: Vysotski | [[Category: Vysotski ES]] | ||
[[Category: Wang | [[Category: Wang BC]] | ||
Latest revision as of 12:51, 28 December 2022
Spatial structure of the novel light-sensitive photoprotein berovin from the ctenophore Beroe abyssicola in the Ca2+-loaded apoprotein conformation stateSpatial structure of the novel light-sensitive photoprotein berovin from the ctenophore Beroe abyssicola in the Ca2+-loaded apoprotein conformation state
Structural highlights
FunctionPublication Abstract from PubMedThe bright bioluminescence of ctenophores, found in oceans worldwide, is determined by Ca(2+)-regulated photoproteins, functionally identical to and sharing many properties of hydromedusan photoproteins. In contrast, however, the ctenophore photoproteins are extremely sensitive to UV and visible light over the range of their absorption spectrum. The spatial structure of a novel light-sensitive photoprotein from the ctenophore Beroe abyssicola in its apoform bound with three calcium ions is determined at 2.0A. We demonstrate that the apoberovin is a slightly asymmetrical compact globular protein formed by two domains with a cavity in the center, which exactly retains the fold architecture characteristic of hydromedusan photoproteins despite their low amino acid sequence identity. However, the structural alignment of these two photoprotein classes clearly shows that despite the high similarity of shape and geometry of their coelenterazine-binding cavities, their interiors differ drastically. The key residues appearing to be crucial for stabilizing the 2-hydroperoxycoelenterazine and for formation of the emitter in hydromedusan photoproteins, are replaced in berovin by amino acid residues having completely different side chain properties. Evidently, these replacements must be responsible for the distinct properties of ctenophore photoproteins such as sensitivity to light or the fact that the formation of active photoprotein from apophotoprotein, coelenterazine, and oxygen is more effective at alkaline pH. Spatial structure of the novel light-sensitive photoprotein berovin from the ctenophore Beroe abyssicola in the Ca(2+)-loaded apoprotein conformation state.,Stepanyuk GA, Liu ZJ, Burakova LP, Lee J, Rose J, Vysotski ES, Wang BC Biochim Biophys Acta. 2013 Oct;1834(10):2139-46. doi:, 10.1016/j.bbapap.2013.07.006. Epub 2013 Jul 25. PMID:23891746[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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