1luc
From Proteopedia
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|PDB= 1luc |SIZE=350|CAPTION= <scene name='initialview01'>1luc</scene>, resolution 1.5Å | |PDB= 1luc |SIZE=350|CAPTION= <scene name='initialview01'>1luc</scene>, resolution 1.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1luc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1luc OCA], [http://www.ebi.ac.uk/pdbsum/1luc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1luc RCSB]</span> | ||
}} | }} | ||
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[[Category: Fisher, A J.]] | [[Category: Fisher, A J.]] | ||
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: MG]] | ||
[[Category: flavoprotein]] | [[Category: flavoprotein]] | ||
[[Category: monooxygenase]] | [[Category: monooxygenase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:07:32 2008'' |
Revision as of 19:07, 30 March 2008
| |||||||
| , resolution 1.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Alkanal monooxygenase (FMN-linked), with EC number 1.14.14.3 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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