2d1q | pdb_00002d1q

Crystal structure of the thermostable Japanese Firefly Luciferase complexed with MgATP

spinqualitylabelsall models 2d1q, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2d1q is a 1 chain structure with sequence from Genji firefly. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AMP NonStd Res: CSO Related: 2d1s, 2d1r, 2d1t Activity: Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing), with EC number 1.13.12.7 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Function [LUCI_LUCCR] Produces green light with a wavelength of 544 nm. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Luciferase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA