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[[Image:3b9n.jpg|left|200px]]


{{Structure
==Crystal structure of long-chain alkane monooxygenase (LadA)==
|PDB= 3b9n |SIZE=350|CAPTION= <scene name='initialview01'>3b9n</scene>, resolution 2.7&Aring;
<StructureSection load='3b9n' size='340' side='right'caption='[[3b9n]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[3b9n]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_thermodenitrificans Geobacillus thermodenitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B9N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B9N FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
|GENE= ladA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33940 Geobacillus thermodenitrificans])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b9n OCA], [https://pdbe.org/3b9n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b9n RCSB], [https://www.ebi.ac.uk/pdbsum/3b9n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b9n ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=[[3b9o|3B9O]]
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3b9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b9n OCA], [http://www.ebi.ac.uk/pdbsum/3b9n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3b9n RCSB]</span>
[https://www.uniprot.org/uniprot/LADA_GEOTN LADA_GEOTN] Involved in the degradation of long-chain alkanes (PubMed:17372208, PubMed:22526792). Converts alkanes ranging from C(15) to C(36) into their corresponding primary alcohols (PubMed:17372208).<ref>PMID:17372208</ref> <ref>PMID:22526792</ref>
}}
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
'''Crystal structure of long-chain alkane monooxygenase (LadA)'''
Check<jmol>
 
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b9/3b9n_consurf.spt"</scriptWhenChecked>
==Overview==
    <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=3b9n ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
LadA, a long-chain alkane monooxygenase, utilizes a terminal oxidation pathway for the conversion of long-chain alkanes (up to at least C(36)) to corresponding primary alcohols in thermophilic bacillus Geobacillus thermodenitrificans NG80-2. Here, we report the first structure of the long-chain alkane hydroxylase, LadA, and its complex with the flavin mononucleotide (FMN) coenzyme. LadA is characterized as a new member of the SsuD subfamily of the bacterial luciferase family via a surprising structural relationship. The LadA:FMN binary complex structure and a LadA:FMN:alkane model reveal a hydrophobic cavity that has dual roles: to provide a hydrogen-bond donor (His138) for catalysis and to create a solvent-free environment in which to stabilize the C4a-hydroperoxyflavin intermediate. Consequently, LadA should catalyze the conversion of long-chain alkanes via the acknowledged flavoprotein monooxygenase mechanism. This finding suggests that the ability of LadA to catalyze the degradation of long-chain alkanes is determined by the binding mode of the long-chain alkane substrates. The LadA structure opens a rational perspective to explore and alter the substrate binding site of LadA, with potential biotechnological applications in areas such as petroleum exploration and treatment of environmental oil pollution.
LadA, a long-chain alkane monooxygenase, utilizes a terminal oxidation pathway for the conversion of long-chain alkanes (up to at least C(36)) to corresponding primary alcohols in thermophilic bacillus Geobacillus thermodenitrificans NG80-2. Here, we report the first structure of the long-chain alkane hydroxylase, LadA, and its complex with the flavin mononucleotide (FMN) coenzyme. LadA is characterized as a new member of the SsuD subfamily of the bacterial luciferase family via a surprising structural relationship. The LadA:FMN binary complex structure and a LadA:FMN:alkane model reveal a hydrophobic cavity that has dual roles: to provide a hydrogen-bond donor (His138) for catalysis and to create a solvent-free environment in which to stabilize the C4a-hydroperoxyflavin intermediate. Consequently, LadA should catalyze the conversion of long-chain alkanes via the acknowledged flavoprotein monooxygenase mechanism. This finding suggests that the ability of LadA to catalyze the degradation of long-chain alkanes is determined by the binding mode of the long-chain alkane substrates. The LadA structure opens a rational perspective to explore and alter the substrate binding site of LadA, with potential biotechnological applications in areas such as petroleum exploration and treatment of environmental oil pollution.


==About this Structure==
Crystal structure of long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN: unveiling the long-chain alkane hydroxylase.,Li L, Liu X, Yang W, Xu F, Wang W, Feng L, Bartlam M, Wang L, Rao Z J Mol Biol. 2008 Feb 15;376(2):453-65. Epub 2007 Nov 28. PMID:18164311<ref>PMID:18164311</ref>
3B9N is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_thermodenitrificans Geobacillus thermodenitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3B9N OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure of long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN: unveiling the long-chain alkane hydroxylase., Li L, Liu X, Yang W, Xu F, Wang W, Feng L, Bartlam M, Wang L, Rao Z, J Mol Biol. 2008 Feb 15;376(2):453-65. Epub 2007 Nov 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18164311 18164311]
</div>
<div class="pdbe-citations 3b9n" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Geobacillus thermodenitrificans]]
[[Category: Geobacillus thermodenitrificans]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bartlam, M.]]
[[Category: Bartlam M]]
[[Category: Li, L.]]
[[Category: Li L]]
[[Category: Rao, Z.]]
[[Category: Rao Z]]
[[Category: Xu, F.]]
[[Category: Xu F]]
[[Category: Yang, W.]]
[[Category: Yang W]]
[[Category: alkane hydroxylase]]
[[Category: crystal structure]]
[[Category: geobacillus thermodenitrifican]]
[[Category: lada]]
[[Category: monooxygenase]]
[[Category: oxidoreductase]]
[[Category: plasmid]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:24:24 2008''

Latest revision as of 14:42, 1 November 2023

Crystal structure of long-chain alkane monooxygenase (LadA)

3b9n, resolution 2.70Å

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