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| - | [[Image:1luc.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1luc| PDB=1luc | SCENE= }} | | {{STRUCTURE_1luc| PDB=1luc | SCENE= }} |
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| - | '''BACTERIAL LUCIFERASE'''
| + | ===BACTERIAL LUCIFERASE=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8703001}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8703001 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8703001}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Flavoprotein]] | | [[Category: Flavoprotein]] |
| | [[Category: Monooxygenase]] | | [[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 Wed Jul 2 22:15:58 2008'' |
Revision as of 19:16, 2 July 2008
Template:STRUCTURE 1luc
BACTERIAL LUCIFERASE
Template:ABSTRACT PUBMED 8703001
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
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