1luc
From Proteopedia
(New page: 200px<br /><applet load="1luc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1luc, resolution 1.5Å" /> '''BACTERIAL LUCIFERASE'...) |
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| - | [[Image:1luc.jpg|left|200px]]<br /><applet load="1luc" size=" | + | [[Image:1luc.jpg|left|200px]]<br /><applet load="1luc" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1luc, resolution 1.5Å" /> | caption="1luc, resolution 1.5Å" /> | ||
'''BACTERIAL LUCIFERASE'''<br /> | '''BACTERIAL LUCIFERASE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Bacterial luciferase is a flavin monooxygenase that catalyzes the | + | Bacterial luciferase is a flavin monooxygenase that catalyzes the oxidation of a long-chain aldehyde and releases energy in the form of visible light. A new crystal form of luciferase cloned from Vibrio harveyi has been grown under low-salt concentrations, which diffract x-rays beyond 1.5-A resolution. The x-ray structure of bacterial luciferase has been refined to a conventional R-factor of 18.2% for all recorded synchrotron data between 30.0 and 1.50-A resolution. Bacterial luciferase is an alpha-beta heterodimer, and the individual subunits fold into a single domain (beta/alpha)8 barrel. The high resolution structure reveals a non-prolyl cis peptide bond that forms between Ala74 and Ala75 in the alpha subunit near the putative active site. This cis peptide bond may have functional significance for creating a cavity at the active site. Bacterial luciferase employs reduced flavin as a substrate rather than a cofactor. The structure presented was determined in the absence of substrates. A comparison of the structural similarities between luciferase and a nonfluorescent flavoprotein, which is expressed in the lux operon of one genus of bioluminescent bacteria, suggests that the two proteins originated from a common ancestor. However, the flavin binding sites of the nonfluorescent protein are likely not representative of the flavin binding site on luciferase. The structure presented here will furnish a detailed molecular model for all bacterial luciferases. |
==About this Structure== | ==About this Structure== | ||
| - | 1LUC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi] with MG and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alkanal_monooxygenase_(FMN-linked) Alkanal monooxygenase (FMN-linked)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.3 1.14.14.3] Full crystallographic information is available from [http:// | + | 1LUC is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alkanal_monooxygenase_(FMN-linked) Alkanal monooxygenase (FMN-linked)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.3 1.14.14.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LUC OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Vibrio harveyi]] | [[Category: Vibrio harveyi]] | ||
| - | [[Category: Fisher, A | + | [[Category: Fisher, A J.]] |
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
[[Category: EDO]] | [[Category: EDO]] | ||
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[[Category: monooxygenase]] | [[Category: monooxygenase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:34 2008'' |
Revision as of 11:48, 21 February 2008
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BACTERIAL LUCIFERASE
Overview
Bacterial luciferase is a flavin monooxygenase that catalyzes the oxidation of a long-chain aldehyde and releases energy in the form of visible light. A new crystal form of luciferase cloned from Vibrio harveyi has been grown under low-salt concentrations, which diffract x-rays beyond 1.5-A resolution. The x-ray structure of bacterial luciferase has been refined to a conventional R-factor of 18.2% for all recorded synchrotron data between 30.0 and 1.50-A resolution. Bacterial luciferase is an alpha-beta heterodimer, and the individual subunits fold into a single domain (beta/alpha)8 barrel. The high resolution structure reveals a non-prolyl cis peptide bond that forms between Ala74 and Ala75 in the alpha subunit near the putative active site. This cis peptide bond may have functional significance for creating a cavity at the active site. Bacterial luciferase employs reduced flavin as a substrate rather than a cofactor. The structure presented was determined in the absence of substrates. A comparison of the structural similarities between luciferase and a nonfluorescent flavoprotein, which is expressed in the lux operon of one genus of bioluminescent bacteria, suggests that the two proteins originated from a common ancestor. However, the flavin binding sites of the nonfluorescent protein are likely not representative of the flavin binding site on luciferase. The structure presented here will furnish a detailed molecular model for all bacterial luciferases.
About this Structure
1LUC is a Protein complex structure of sequences from Vibrio harveyi with and as ligands. Active as Alkanal monooxygenase (FMN-linked), with EC number 1.14.14.3 Full crystallographic information is available from OCA.
Reference
The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions., Fisher AJ, Thompson TB, Thoden JB, Baldwin TO, Rayment I, J Biol Chem. 1996 Sep 6;271(36):21956-68. PMID:8703001
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