1lci
From Proteopedia
(New page: 200px<br /><applet load="1lci" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lci, resolution 2.0Å" /> '''FIREFLY LUCIFERASE'''...) |
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| - | [[Image:1lci.jpg|left|200px]]<br /><applet load="1lci" size=" | + | [[Image:1lci.jpg|left|200px]]<br /><applet load="1lci" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lci, resolution 2.0Å" /> | caption="1lci, resolution 2.0Å" /> | ||
'''FIREFLY LUCIFERASE'''<br /> | '''FIREFLY LUCIFERASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND. Firefly luciferase is a 62 kDa protein that catalyzes the | + | BACKGROUND. Firefly luciferase is a 62 kDa protein that catalyzes the production of light. In the presence of MgATP and molecular oxygen, the enzyme oxidizes its substrate, firefly luciferin, emitting yellow-green light. The reaction proceeds through activation of the substrate to form an adenylate intermediate. Firefly luciferase shows extensive sequence homology with a number of enzymes that utilize ATP in adenylation reactions. RESULTS. We have determined the crystal structure of firefly luciferase at 2.0 A resolution. The protein is folded into two compact domains. The large N-terminal domain consists of a beta-barrel and two beta-sheets. The sheets are flanked by alpha-helices to form an alphabetaalphabetaalpha five-layered structure. The C-terminal portion of the molecule forms a distinct domain, which is separated from the N-terminal domain by a wide cleft. CONCLUSIONS. Firefly luciferase is the first member of a superfamily of homologous enzymes, which includes acyl-coenzyme A ligases and peptide synthetases, to have its structure characterized. The residues conserved within the superfamily are located on the surfaces of the two domains on either side of the cleft, but are too far apart to interact simultaneously with the substrates. This suggests that the two domains will close in the course of the reaction. Firefly luciferase has a novel structural framework for catalyzing adenylate-forming reactions. |
==About this Structure== | ==About this Structure== | ||
| - | 1LCI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Photinus_pyralis Photinus pyralis]. Active as [http://en.wikipedia.org/wiki/Photinus-luciferin_4-monooxygenase_(ATP-hydrolyzing) Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.12.7 1.13.12.7] Full crystallographic information is available from [http:// | + | 1LCI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Photinus_pyralis Photinus pyralis]. Active as [http://en.wikipedia.org/wiki/Photinus-luciferin_4-monooxygenase_(ATP-hydrolyzing) Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.12.7 1.13.12.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LCI OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Brick, P.]] | [[Category: Brick, P.]] | ||
[[Category: Conti, E.]] | [[Category: Conti, E.]] | ||
| - | [[Category: Franks, N | + | [[Category: Franks, N P.]] |
[[Category: luminescence]] | [[Category: luminescence]] | ||
[[Category: monooxygenase]] | [[Category: monooxygenase]] | ||
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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 13:43:40 2008'' |
Revision as of 11:43, 21 February 2008
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FIREFLY LUCIFERASE
Overview
BACKGROUND. Firefly luciferase is a 62 kDa protein that catalyzes the production of light. In the presence of MgATP and molecular oxygen, the enzyme oxidizes its substrate, firefly luciferin, emitting yellow-green light. The reaction proceeds through activation of the substrate to form an adenylate intermediate. Firefly luciferase shows extensive sequence homology with a number of enzymes that utilize ATP in adenylation reactions. RESULTS. We have determined the crystal structure of firefly luciferase at 2.0 A resolution. The protein is folded into two compact domains. The large N-terminal domain consists of a beta-barrel and two beta-sheets. The sheets are flanked by alpha-helices to form an alphabetaalphabetaalpha five-layered structure. The C-terminal portion of the molecule forms a distinct domain, which is separated from the N-terminal domain by a wide cleft. CONCLUSIONS. Firefly luciferase is the first member of a superfamily of homologous enzymes, which includes acyl-coenzyme A ligases and peptide synthetases, to have its structure characterized. The residues conserved within the superfamily are located on the surfaces of the two domains on either side of the cleft, but are too far apart to interact simultaneously with the substrates. This suggests that the two domains will close in the course of the reaction. Firefly luciferase has a novel structural framework for catalyzing adenylate-forming reactions.
About this Structure
1LCI is a Single protein structure of sequence from Photinus pyralis. Active as Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing), with EC number 1.13.12.7 Full crystallographic information is available from OCA.
Reference
Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes., Conti E, Franks NP, Brick P, Structure. 1996 Mar 15;4(3):287-98. PMID:8805533
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