1qv0
From Proteopedia
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| , resolution 1.10Å | |||||||
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| Ligands: | , , , | ||||||
| Activity: | Renilla-luciferin 2-monooxygenase, with EC number 1.13.12.5 | ||||||
| Related: | 1EL4, 1EJ3, 1JF0, 1JF2, 1QV1
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Sun Mar 30 23:19:25 2008
