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[[Image:1luc.jpg|left|200px]]


{{Structure
==BACTERIAL LUCIFERASE==
|PDB= 1luc |SIZE=350|CAPTION= <scene name='initialview01'>1luc</scene>, resolution 1.5&Aring;
<StructureSection load='1luc' size='340' side='right'caption='[[1luc]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
<table><tr><td colspan='2'>[[1luc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LUC FirstGlance]. <br>
|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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1luc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1luc OCA], [https://pdbe.org/1luc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1luc RCSB], [https://www.ebi.ac.uk/pdbsum/1luc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1luc ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|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>
== Function ==
}}
[https://www.uniprot.org/uniprot/LUXA_VIBHA LUXA_VIBHA] Light-emitting reaction in luminous bacteria.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lu/1luc_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1luc ConSurf].
<div style="clear:both"></div>


'''BACTERIAL LUCIFERASE'''
==See Also==
 
*[[Luciferase 3D structures|Luciferase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
==About this Structure==
1LUC is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LUC 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:[http://www.ncbi.nlm.nih.gov/pubmed/8703001 8703001]
[[Category: Alkanal monooxygenase (FMN-linked)]]
[[Category: Protein complex]]
[[Category: Vibrio harveyi]]
[[Category: Vibrio harveyi]]
[[Category: Fisher, A J.]]
[[Category: Fisher AJ]]
[[Category: Rayment, I.]]
[[Category: Rayment I]]
[[Category: flavoprotein]]
[[Category: monooxygenase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:07:32 2008''

Latest revision as of 10:36, 14 February 2024

BACTERIAL LUCIFERASEBACTERIAL LUCIFERASE

Structural highlights

1luc is a 2 chain structure with sequence from Vibrio harveyi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LUXA_VIBHA Light-emitting reaction in luminous bacteria.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1luc, resolution 1.50Å

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