2d1q

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[[Image:2d1q.gif|left|200px]]<br /><applet load="2d1q" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2d1q.gif|left|200px]]
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caption="2d1q, resolution 2.30&Aring;" />
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'''Crystal structure of the thermostable Japanese Firefly Luciferase complexed with MgATP'''<br />
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{{Structure
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|PDB= 2d1q |SIZE=350|CAPTION= <scene name='initialview01'>2d1q</scene>, resolution 2.30&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=AMP:ADENOSINE MONOPHOSPHATE'>AMP</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''Crystal structure of the thermostable Japanese Firefly Luciferase complexed with MgATP'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2D1Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Luciola_cruciata Luciola cruciata] with <scene name='pdbligand=AMP:'>AMP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=2D1Q OCA].
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2D1Q is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Luciola_cruciata Luciola cruciata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D1Q OCA].
==Reference==
==Reference==
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Structural basis for the spectral difference in luciferase bioluminescence., Nakatsu T, Ichiyama S, Hiratake J, Saldanha A, Kobashi N, Sakata K, Kato H, Nature. 2006 Mar 16;440(7082):372-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16541080 16541080]
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Structural basis for the spectral difference in luciferase bioluminescence., Nakatsu T, Ichiyama S, Hiratake J, Saldanha A, Kobashi N, Sakata K, Kato H, Nature. 2006 Mar 16;440(7082):372-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16541080 16541080]
[[Category: Luciola cruciata]]
[[Category: Luciola cruciata]]
[[Category: Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing)]]
[[Category: Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing)]]
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[[Category: riken structural genomics/proteomics initiative]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: rsgi]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:22:15 2008''

Revision as of 14:22, 20 March 2008

Image:2d1q.gif


PDB ID 2d1q

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands:
Activity: Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing), with EC number 1.13.12.7
Coordinates: save as pdb, mmCIF, xml



Crystal structure of the thermostable Japanese Firefly Luciferase complexed with MgATP


Overview

Fireflies communicate with each other by emitting yellow-green to yellow-orange brilliant light. The bioluminescence reaction, which uses luciferin, Mg-ATP and molecular oxygen to yield an electronically excited oxyluciferin species, is carried out by the enzyme luciferase. Visible light is emitted during relaxation of excited oxyluciferin to its ground state. The high quantum yield of the luciferin/luciferase reaction and the change in bioluminescence colour caused by subtle structural differences in luciferase have attracted much research interest. In fact, a single amino acid substitution in luciferase changes the emission colour from yellow-green to red. Although the crystal structure of luciferase from the North American firefly (Photinus pyralis) has been described, the detailed mechanism for the bioluminescence colour change is still unclear. Here we report the crystal structures of wild-type and red mutant (S286N) luciferases from the Japanese Genji-botaru (Luciola cruciata) in complex with a high-energy intermediate analogue, 5'-O-[N-(dehydroluciferyl)-sulfamoyl]adenosine (DLSA). Comparing these structures to those of the wild-type luciferase complexed with AMP plus oxyluciferin (products) reveals a significant conformational change in the wild-type enzyme but not in the red mutant. This conformational change involves movement of the hydrophobic side chain of Ile 288 towards the benzothiazole ring of DLSA. Our results indicate that the degree of molecular rigidity of the excited state of oxyluciferin, which is controlled by a transient movement of Ile 288, determines the colour of bioluminescence during the emission reaction.

About this Structure

2D1Q is a Single protein structure of sequence from Luciola cruciata. Full crystallographic information is available from OCA.

Reference

Structural basis for the spectral difference in luciferase bioluminescence., Nakatsu T, Ichiyama S, Hiratake J, Saldanha A, Kobashi N, Sakata K, Kato H, Nature. 2006 Mar 16;440(7082):372-6. PMID:16541080

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