1luc
From Proteopedia
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'''BACTERIAL LUCIFERASE''' | '''BACTERIAL LUCIFERASE''' | ||
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==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/8703001 8703001] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8703001 8703001] | ||
| - | [[Category: Alkanal monooxygenase (FMN-linked)]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Vibrio harveyi]] | [[Category: Vibrio harveyi]] | ||
[[Category: Fisher, A J.]] | [[Category: Fisher, A J.]] | ||
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
| - | [[Category: | + | [[Category: Flavoprotein]] |
| - | [[Category: | + | [[Category: Monooxygenase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:17:50 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 21:17, 2 May 2008
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. 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 Page seeded by OCA on Sat May 3 00:17:50 2008
