|
|
| Line 3: |
Line 3: |
| | <StructureSection load='3b9o' size='340' side='right'caption='[[3b9o]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='3b9o' size='340' side='right'caption='[[3b9o]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3b9o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_thermodenitrificans"_klaushofer_and_hollaus_1970 "bacillus thermodenitrificans" klaushofer and hollaus 1970]. 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> | + | <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> |
| - | </td></tr><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3b9n|3b9n]]</div></td></tr> | + | <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> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ladA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33940 "Bacillus thermodenitrificans" Klaushofer and Hollaus 1970])</td></tr>
| + | |
| | <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> | | <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> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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 == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 32: |
Line 33: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus thermodenitrificans klaushofer and hollaus 1970]] | + | [[Category: Geobacillus thermodenitrificans]] |
| | [[Category: Large Structures]] | | [[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: Geobacillus thermodenitrifican]]
| + | |
| - | [[Category: Lada]]
| + | |
| - | [[Category: Monooxygenase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Plasmid]]
| + | |
| Structural highlights
Function
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).[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Feng L, Wang W, Cheng J, Ren Y, Zhao G, Gao C, Tang Y, Liu X, Han W, Peng X, Liu R, Wang L. Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir. Proc Natl Acad Sci U S A. 2007 Mar 27;104(13):5602-7. PMID:17372208 doi:10.1073/pnas.0609650104
- ↑ Dong Y, Yan J, Du H, Chen M, Ma T, Feng L. Engineering of LadA for enhanced hexadecane oxidation using random site-directed mutagenesis. Appl Microbiol Biotechnol. 2012 May;94(4):1019-29. PMID:22526792 doi:10.1007/s00253-012-4035-y
- ↑ Li L, Liu X, Yang W, Xu F, Wang W, Feng L, Bartlam M, Wang L, Rao Z. Crystal structure of long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN: unveiling the long-chain alkane hydroxylase. J Mol Biol. 2008 Feb 15;376(2):453-65. Epub 2007 Nov 28. PMID:18164311 doi:10.1016/j.jmb.2007.11.069
|
