3b9o

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{{Seed}}
 
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[[Image:3b9o.png|left|200px]]
 
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==long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN==
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The line below this paragraph, containing "STRUCTURE_3b9o", creates the "Structure Box" on the page.
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<StructureSection load='3b9o' size='340' side='right'caption='[[3b9o]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3b9o]] 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=3B9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B9O FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
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{{STRUCTURE_3b9o| PDB=3b9o | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b9o OCA], [https://pdbe.org/3b9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b9o RCSB], [https://www.ebi.ac.uk/pdbsum/3b9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b9o ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b9/3b9o_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3b9o ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_18164311}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3b9o" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18164311 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18164311}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3B9O is a 2 chains structure of sequences 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=3B9O OCA].
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==Reference==
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<ref group="xtra">PMID:18164311</ref><references group="xtra"/>
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[[Category: Geobacillus thermodenitrificans]]
[[Category: Geobacillus thermodenitrificans]]
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[[Category: Bartlam, M.]]
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[[Category: Large Structures]]
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[[Category: Li, L.]]
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[[Category: Bartlam M]]
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[[Category: Rao, Z.]]
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[[Category: Li L]]
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[[Category: Xu, F.]]
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[[Category: Rao Z]]
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[[Category: Yang, W.]]
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[[Category: Xu F]]
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[[Category: Alkane hydroxylase]]
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[[Category: Yang W]]
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[[Category: Crystal structure]]
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[[Category: Geobacillus thermodenitrifican]]
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[[Category: Lada]]
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[[Category: Monooxygenase]]
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[[Category: Oxidoreductase]]
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[[Category: Plasmid]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 02:33:07 2009''
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Current revision

long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN

PDB ID 3b9o

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