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1s36

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{{STRUCTURE_1s36| PDB=1s36 | SCENE= }}
{{STRUCTURE_1s36| PDB=1s36 | SCENE= }}
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'''Crystal structure of a Ca2+-discharged photoprotein: Implications for the mechanisms of the calcium trigger and the bioluminescence'''
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===Crystal structure of a Ca2+-discharged photoprotein: Implications for the mechanisms of the calcium trigger and the bioluminescence===
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==Overview==
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Ca2+-regulated photoproteins are members of the EF-hand calcium-binding protein family. The addition of Ca2+ produces a blue bioluminescence by triggering a decarboxylation reaction of protein-bound hydroperoxycoelenterazine to form the product, coelenteramide, in an excited state. Based on the spatial structures of aequorin and several obelins, we have postulated mechanisms for the Ca2+ trigger and for generation of the different excited states that are the origin of the different colors of bioluminescence. Here we report the crystal structure of the Ca2+-discharged photoprotein obelin at 1.96-A resolution. The results lend support to the proposed mechanisms and provide new structural insight into details of these processes. Global conformational changes caused by Ca2+ association are typical of the class of calcium signal modulators within the EF-hand protein superfamily. Accommodation of the Ca2+ ions into the loops of the EF-hands is seen to propagate into the active site of the protein now occupied by the coelenteramide where there is a significant repositioning and flipping of the His-175 imidazole ring as crucially required in the trigger hypothesis. Also the H-bonding between His-22 and the coelenterazine found in the active photoprotein is preserved at the equivalent position of coelenteramide, confirming the proposed rapid excited state proton transfer that would lead to the excited state of the phenolate ion pair, which is responsible for the blue emission of bioluminescence.
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(as it appears on PubMed at http://www.pubmed.gov), where 15155735 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15155735}}
==About this Structure==
==About this Structure==
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[[Category: Southeast collaboratory for structural genomic]]
[[Category: Southeast collaboratory for structural genomic]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:14:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:42:29 2008''

Revision as of 07:42, 29 July 2008

Image:1s36.png

Template:STRUCTURE 1s36

Crystal structure of a Ca2+-discharged photoprotein: Implications for the mechanisms of the calcium trigger and the bioluminescence

Template:ABSTRACT PUBMED 15155735

About this Structure

1S36 is a Single protein structure of sequence from Obelia longissima. Full crystallographic information is available from OCA.

Reference

Crystal structure of a Ca2+-discharged photoprotein: implications for mechanisms of the calcium trigger and bioluminescence., Deng L, Markova SV, Vysotski ES, Liu ZJ, Lee J, Rose J, Wang BC, J Biol Chem. 2004 Aug 6;279(32):33647-52. Epub 2004 May 20. PMID:15155735

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