1qv0
From Proteopedia
(New page: 200px<br /><applet load="1qv0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qv0, resolution 1.10Å" /> '''Atomic resolution st...) |
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| - | [[Image:1qv0.jpg|left|200px]]<br /><applet load="1qv0" size=" | + | [[Image:1qv0.jpg|left|200px]]<br /><applet load="1qv0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qv0, resolution 1.10Å" /> | caption="1qv0, resolution 1.10Å" /> | ||
'''Atomic resolution structure of obelin from Obelia longissima'''<br /> | '''Atomic resolution structure of obelin from Obelia longissima'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The spatial structure of the Ca(2+)-regulated photoprotein obelin has been | + | The spatial structure of the Ca(2+)-regulated photoprotein obelin has been solved to resolution of 1.1A. Two oxygen atoms are revealed substituted at the C2-position of the coelenterazine in contrast to the obelin structure at 1.73A resolution where one oxygen atom only was disclosed. The electron density of the second oxygen atom was very weak but after exposing the crystals to a trace of Ca(2+), the electron densities of both oxygen atoms became equally intense. In addition, one Ca(2+) was found bound in the loop of the first EF-hand motif. Four of the ligands were provided by protein residues Asp30, Asn32, Asn34, and the main chain oxygen of Lys36. The other two were from water molecules. From a comparison of B-factors for the residues constituting the active site, it is suggested that the variable electron densities observed in various photoprotein structures could be attributed to different mobilities of the peroxy oxygen atoms. |
==About this Structure== | ==About this Structure== | ||
| - | 1QV0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Obelia_longissima Obelia longissima] with CO, K, CZH and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Renilla-luciferin_2-monooxygenase Renilla-luciferin 2-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.12.5 1.13.12.5] Full crystallographic information is available from [http:// | + | 1QV0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Obelia_longissima Obelia longissima] with <scene name='pdbligand=CO:'>CO</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=CZH:'>CZH</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Renilla-luciferin_2-monooxygenase Renilla-luciferin 2-monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.12.5 1.13.12.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QV0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Deng, L.]] | [[Category: Deng, L.]] | ||
[[Category: Lee, J.]] | [[Category: Lee, J.]] | ||
| - | [[Category: Liu, Z | + | [[Category: Liu, Z J.]] |
[[Category: Rose, J.]] | [[Category: Rose, J.]] | ||
| - | [[Category: Vysotski, E | + | [[Category: Vysotski, E S.]] |
| - | [[Category: Wang, B | + | [[Category: Wang, B C.]] |
[[Category: CO]] | [[Category: CO]] | ||
[[Category: CZH]] | [[Category: CZH]] | ||
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[[Category: photoprotein]] | [[Category: photoprotein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:43:59 2008'' |
Revision as of 12:44, 21 February 2008
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Atomic resolution structure of obelin from Obelia longissima
Overview
The spatial structure of the Ca(2+)-regulated photoprotein obelin has been solved to resolution of 1.1A. Two oxygen atoms are revealed substituted at the C2-position of the coelenterazine in contrast to the obelin structure at 1.73A resolution where one oxygen atom only was disclosed. The electron density of the second oxygen atom was very weak but after exposing the crystals to a trace of Ca(2+), the electron densities of both oxygen atoms became equally intense. In addition, one Ca(2+) was found bound in the loop of the first EF-hand motif. Four of the ligands were provided by protein residues Asp30, Asn32, Asn34, and the main chain oxygen of Lys36. The other two were from water molecules. From a comparison of B-factors for the residues constituting the active site, it is suggested that the variable electron densities observed in various photoprotein structures could be attributed to different mobilities of the peroxy oxygen atoms.
About this Structure
1QV0 is a Single protein structure of sequence from Obelia longissima with , , and as ligands. Active as Renilla-luciferin 2-monooxygenase, with EC number 1.13.12.5 Full crystallographic information is available from OCA.
Reference
Atomic resolution structure of obelin: soaking with calcium enhances electron density of the second oxygen atom substituted at the C2-position of coelenterazine., Liu ZJ, Vysotski ES, Deng L, Lee J, Rose J, Wang BC, Biochem Biophys Res Commun. 2003 Nov 14;311(2):433-9. PMID:14592432
Page seeded by OCA on Thu Feb 21 14:43:59 2008
Categories: Obelia longissima | Renilla-luciferin 2-monooxygenase | Single protein | Deng, L. | Lee, J. | Liu, Z J. | Rose, J. | Vysotski, E S. | Wang, B C. | CO | CZH | GOL | K | Atomic resolution | Bioluminescence | Calcium binding | Crystal structure | Ef-hand | Obelin | Photoprotein
