2d1q
From Proteopedia
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|PDB= 2d1q |SIZE=350|CAPTION= <scene name='initialview01'>2d1q</scene>, resolution 2.30Å | |PDB= 2d1q |SIZE=350|CAPTION= <scene name='initialview01'>2d1q</scene>, resolution 2.30Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=AMP:ADENOSINE MONOPHOSPHATE'>AMP</scene> | + | |LIGAND= <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene> |
| - | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2d1s|2D1S]], [[2d1r|2D1R]], [[2d1t|2D1T]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d1q OCA], [http://www.ebi.ac.uk/pdbsum/2d1q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d1q RCSB]</span> | ||
}} | }} | ||
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[[Category: Sakata, K.]] | [[Category: Sakata, K.]] | ||
[[Category: Saldanha, A.]] | [[Category: Saldanha, A.]] | ||
| - | [[Category: AMP]] | ||
[[Category: alpha+beta]] | [[Category: alpha+beta]] | ||
[[Category: alpha/beta]] | [[Category: alpha/beta]] | ||
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[[Category: structural genomic]] | [[Category: structural genomic]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:29:05 2008'' |
Revision as of 23:29, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing), with EC number 1.13.12.7 | ||||||
| Related: | 2D1S, 2D1R, 2D1T
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Mon Mar 31 02:29:05 2008
Categories: Luciola cruciata | Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing) | Single protein | Hiratake, J. | Ichiyama, S. | Kato, H. | Kobashi, N. | Nakatsu, T. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Sakata, K. | Saldanha, A. | Alpha+beta | Alpha/beta | Beta barrel | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic
