1sl7

From Proteopedia

(Difference between revisions)

Revision as of 07:33, 22 September 2021

Crystal structure of calcium-loaded apo-obelin from Obelia longissima

Structural highlights

1sl7 is a 1 chain structure with sequence from Black sea hydrozoan. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1el4, 1ej3, 1jf0, 1jf2, 1qv0, 1qv1, 1s36
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[OBL_OBELO] Ca(2+)-dependent bioluminescence photoprotein. Displays an emission peak at 470 nm (blue light). Trace amounts of calcium ion trigger the intramolecular oxidation of the chromophore, coelenterazine into coelenteramide and CO(2) with the concomitant emission of light.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structures of calcium-loaded apo-aequorin and apo-obelin have been determined at resolutions 1.7A and 2.2 A, respectively. A calcium ion is observed in each of the three EF-hand loops that have the canonical calcium-binding sequence, and each is coordinated in the characteristic pentagonal bipyramidal configuration. The calcium-loaded apo-protein retain the same compact scaffold and overall fold as the unreacted photoproteins containing the bound substrate, 2-hyroperoxycoelenterazine, and also the same as the Ca2+-discharged obelin bound with product, coleneteramide. Nevertheless, there are easily discerned shifts in both helix and loop regions, and the shifts are not the same between the two proteins. It is suggested that these photoproteins to sense Ca2+ concentration transients and to produce their bioluminescence response on the millisecond timescale. A mechanism of intrastructural transmission of the calcium signal is proposed.

All three Ca2+-binding loops of photoproteins bind calcium ions: the crystal structures of calcium-loaded apo-aequorin and apo-obelin.,Deng L, Vysotski ES, Markova SV, Liu ZJ, Lee J, Rose J, Wang BC Protein Sci. 2005 Mar;14(3):663-75. Epub 2005 Feb 2. PMID:15689515^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Deng L, Vysotski ES, Markova SV, Liu ZJ, Lee J, Rose J, Wang BC. All three Ca2+-binding loops of photoproteins bind calcium ions: the crystal structures of calcium-loaded apo-aequorin and apo-obelin. Protein Sci. 2005 Mar;14(3):663-75. Epub 2005 Feb 2. PMID:15689515 doi:10.1110/ps.041142905

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1sl7"

@@ Line 3: / Line 3: @@
 <StructureSection load='1sl7' size='340' side='right'caption='[[1sl7]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1sl7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Black_sea_hydrozoan Black sea hydrozoan]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SL7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SL7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1sl7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Black_sea_hydrozoan Black sea hydrozoan]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SL7 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+</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></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1el4|1el4]], [[1ej3|1ej3]], [[1jf0|1jf0]], [[1jf2|1jf2]], [[1qv0|1qv0]], [[1qv1|1qv1]], [[1s36|1s36]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1el4|1el4]], [[1ej3|1ej3]], [[1jf0|1jf0]], [[1jf2|1jf2]], [[1qv0|1qv0]], [[1qv1|1qv1]], [[1s36|1s36]]</div></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=1sl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sl7 OCA], [http://pdbe.org/1sl7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sl7 RCSB], [http://www.ebi.ac.uk/pdbsum/1sl7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sl7 ProSAT], [http://www.topsan.org/Proteins/SECSG/1sl7 TOPSAN]</span></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=1sl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sl7 OCA], [https://pdbe.org/1sl7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sl7 RCSB], [https://www.ebi.ac.uk/pdbsum/1sl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sl7 ProSAT], [https://www.topsan.org/Proteins/SECSG/1sl7 TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/OBL_OBELO OBL_OBELO]] Ca(2+)-dependent bioluminescence photoprotein. Displays an emission peak at 470 nm (blue light). Trace amounts of calcium ion trigger the intramolecular oxidation of the chromophore, coelenterazine into coelenteramide and CO(2) with the concomitant emission of light.
+[[https://www.uniprot.org/uniprot/OBL_OBELO OBL_OBELO]] Ca(2+)-dependent bioluminescence photoprotein. Displays an emission peak at 470 nm (blue light). Trace amounts of calcium ion trigger the intramolecular oxidation of the chromophore, coelenterazine into coelenteramide and CO(2) with the concomitant emission of light.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1sl7

From Proteopedia

Revision as of 07:33, 22 September 2021

Crystal structure of calcium-loaded apo-obelin from Obelia longissima

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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