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4n1g

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Revision as of 12:52, 4 August 2016

Crystal Structure of Ca(2+)- discharged F88Y obelin mutant from Obelia longissima at 1.50 Angstrom resolution

Structural highlights

4n1g is a 2 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:	2f8p, 1qv0, 1jf2, 1s36, 1sl7, 1ej3, 4n1f
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

Publication Abstract from PubMed

Ca2+ -regulated photoproteins are responsible for the bioluminescence of a variety of marine coelenterates. All hydromedusan photoproteins are a single-chain polypeptide to which 2-hydroperoxycoelenterazine is tightly but non-covalently bound. Bioluminescence results from oxidative decarboxylation of 2-hydroperoxycoelenterazine, generating protein-bound coelenteramide in an excited state. The bioluminescence spectral maxima of recombinant photoproteins vary in the range 462-495 nm, despite a high degree of identity of amino acid sequences and spatial structures of these photoproteins. Based on studies of obelin and aequorin mutants with substitution of Phe to Tyr and Tyr to Phe, respectively [Stepanyuk GA et al. (2005) FEBS Lett 579, 1008-1014], it was suggested that the spectral differences may be accounted for by an additional hydrogen bond between the hydroxyl group of a Tyr residue and an oxygen atom of the 6-(p-hydroxyphenyl) substituent of coelenterazine. Here, we report the crystal structures of two conformation states of the F88Y obelin mutant that has bioluminescence and product fluorescence spectra resembling those of aequorin. Comparison of spatial structures of the F88Y obelin conformation states with those of wild-type obelin clearly shows that substitution of Phe to Tyr does not affect the overall structures of either F88Y obelin or its product following Ca2+ discharge, compared to the conformation states of wild-type obelin. The hydrogen bond network in F88Y obelin being due to the Tyr substitution clearly supports the suggestion that different hydrogen bond patterns near the oxygen of the 6-(p-hydroxyphenyl) substituent are the basis for spectral modifications between hydromedusan photoproteins.

Crystal structures of the F88Y obelin mutant before and after bioluminescence provide molecular insight into spectral tuning among hydromedusan photoproteins.,Natashin PV, Markova SV, Lee J, Vysotski ES, Liu ZJ FEBS J. 2014 Jan 13. doi: 10.1111/febs.12715. PMID:24418253^[1]

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

References

↑ Natashin PV, Markova SV, Lee J, Vysotski ES, Liu ZJ. Crystal structures of the F88Y obelin mutant before and after bioluminescence provide molecular insight into spectral tuning among hydromedusan photoproteins. FEBS J. 2014 Jan 13. doi: 10.1111/febs.12715. PMID:24418253 doi:http://dx.doi.org/10.1111/febs.12715

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4n1g"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of Ca(2+)- discharged F88Y obelin mutant from Obelia longissima at 1.50 Angstrom resolution==
 <StructureSection load='4n1g' size='340' side='right' caption='[[4n1g]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CEI:N-[3-BENZYL-5-(4-HYDROXYPHENYL)PYRAZIN-2-YL]-2-(4-HYDROXYPHENYL)ACETAMIDE'>CEI</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2f8p|2f8p]], [[1qv0|1qv0]], [[1jf2|1jf2]], [[1s36|1s36]], [[1sl7|1sl7]], [[1ej3|1ej3]], [[4n1f|4n1f]]</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=4n1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n1g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n1g RCSB], [http://www.ebi.ac.uk/pdbsum/4n1g PDBsum]</span></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=4n1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n1g OCA], [http://pdbe.org/4n1g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n1g RCSB], [http://www.ebi.ac.uk/pdbsum/4n1g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n1g ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4n1g" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4n1g

From Proteopedia

Revision as of 12:52, 4 August 2016

Crystal Structure of Ca(2+)- discharged F88Y obelin mutant from Obelia longissima at 1.50 Angstrom resolution

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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