5g1u

From Proteopedia

(Difference between revisions)

Current revision

Linalool Dehydratase Isomerase in complex with Geraniol

Structural highlights

5g1u is a 5 chain structure with sequence from Castellaniella defragrans 65Phen. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.57Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LDI_CASD6 Anaerobically catalyzes the stereospecific hydration of beta-myrcene to (3S)-linalool and the isomerization of (3S)-linalool to geraniol (PubMed:20663876, PubMed:28068311, Ref.8). Is thus involved in the initial steps of the anaerobic degradation of the monoterpene beta-myrcene (PubMed:20663876). Also catalyzes the reverse reactions, i.e. the isomerization of geraniol to linalool and the dehydration of linalool to myrcene (PubMed:20663876, PubMed:28068311, Ref.8). In this direction, the formation of myrcene from geraniol may be seen as a detoxification process for the monoterpene alcohol (PubMed:20663876). Shows a relatively broad substrate specificity and can use various geraniol and linalool derivatives (PubMed:28068311). Substrates required a specific alpha-methylallyl alcohol signature motif (PubMed:28068311). Neither the monoterpenes alpha- and beta-ocimene nor the monoterpenoids citronellol and nerol can be used as substrates (PubMed:20663876).^[1] ^[2] [REFERENCE:8]

Publication Abstract from PubMed

The asymmetric dehydration of alcohols is an important process for the direct synthesis of alkenes. We report the structure and substrate specificity of the bifunctional linalool dehydratase isomerase (LinD) from the bacterium Castellaniella defragrans that catalyzes in nature the hydration of beta-myrcene to linalool and the subsequent isomerization to geraniol. Enzymatic kinetic resolutions of truncated and elongated aromatic and aliphatic tertiary alcohols (C5-C15) that contain a specific signature motif demonstrate the broad substrate specificity of LinD. The three-dimensional structure of LinD from Castellaniella defragrans revealed a pentamer with active sites at the protomer interfaces. Furthermore, the structure of LinD in complex with the product geraniol provides initial mechanistic insights into this bifunctional enzyme. Site-directed mutagenesis confirmed active site amino acid residues essential for its dehydration and isomerization activity. These structural and mechanistic insights facilitate the development of hydrating catalysts, enriching the toolbox for novel bond-forming biocatalysis.

Structural and functional insights into asymmetric enzymatic dehydration of alkenols.,Nestl BM, Geinitz C, Popa S, Rizek S, Haselbeck RJ, Stephen R, Noble MA, Fischer MP, Ralph EC, Hau HT, Man H, Omar M, Turkenburg JP, van Dien S, Culler SJ, Grogan G, Hauer B Nat Chem Biol. 2017 Jan 9. doi: 10.1038/nchembio.2271. PMID:28068311^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Brodkorb D, Gottschall M, Marmulla R, Luddeke F, Harder J. Linalool dehydratase-isomerase, a bifunctional enzyme in the anaerobic degradation of monoterpenes. J Biol Chem. 2010 Oct 1;285(40):30436-42. doi: 10.1074/jbc.M109.084244. Epub 2010, Jul 27. PMID:20663876 doi:http://dx.doi.org/10.1074/jbc.M109.084244
↑ Nestl BM, Geinitz C, Popa S, Rizek S, Haselbeck RJ, Stephen R, Noble MA, Fischer MP, Ralph EC, Hau HT, Man H, Omar M, Turkenburg JP, van Dien S, Culler SJ, Grogan G, Hauer B. Structural and functional insights into asymmetric enzymatic dehydration of alkenols. Nat Chem Biol. 2017 Jan 9. doi: 10.1038/nchembio.2271. PMID:28068311 doi:http://dx.doi.org/10.1038/nchembio.2271
↑ Nestl BM, Geinitz C, Popa S, Rizek S, Haselbeck RJ, Stephen R, Noble MA, Fischer MP, Ralph EC, Hau HT, Man H, Omar M, Turkenburg JP, van Dien S, Culler SJ, Grogan G, Hauer B. Structural and functional insights into asymmetric enzymatic dehydration of alkenols. Nat Chem Biol. 2017 Jan 9. doi: 10.1038/nchembio.2271. PMID:28068311 doi:http://dx.doi.org/10.1038/nchembio.2271

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5g1u"

@@ Line 3: / Line 3: @@
 <StructureSection load='5g1u' size='340' side='right'caption='[[5g1u]], [[Resolution|resolution]] 2.57&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5g1u]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Castellaniella_defragrans_65phen Castellaniella defragrans 65phen]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G1U OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5G1U FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5g1u]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Castellaniella_defragrans_65Phen Castellaniella defragrans 65Phen]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G1U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G1U FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=64Z:GERANIOL'>64Z</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]] 2.57&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=64Z:GERANIOL'>64Z</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5g1v|5g1v]], [[5g1w|5g1w]]</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=5g1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g1u OCA], [https://pdbe.org/5g1u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g1u RCSB], [https://www.ebi.ac.uk/pdbsum/5g1u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g1u ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5g1u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g1u OCA], [http://pdbe.org/5g1u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g1u RCSB], [http://www.ebi.ac.uk/pdbsum/5g1u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g1u ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/LDI_CASDE LDI_CASDE]] Anaerobically catalyzes the stereospecific hydration of beta-myrcene to (3S)-linalool and the isomerization of (3S)-linalool to geraniol. Is thus involved in the initial steps of the anaerobic degradation of the monoterpene beta-myrcene. Also catalyzes the reverse reactions, i.e. the isomerization of geraniol to linalool and the dehydration of linalool to myrcene. In this direction, the formation of myrcene from geraniol may be seen as a detoxification process for the monoterpene alcohol. Neither the monoterpenes alpha- and beta-ocimene nor the monoterpenoids citronellol and nerol can be used as substrates.<ref>PMID:20663876</ref>
+[https://www.uniprot.org/uniprot/LDI_CASD6 LDI_CASD6] Anaerobically catalyzes the stereospecific hydration of beta-myrcene to (3S)-linalool and the isomerization of (3S)-linalool to geraniol (PubMed:20663876, PubMed:28068311, Ref.8). Is thus involved in the initial steps of the anaerobic degradation of the monoterpene beta-myrcene (PubMed:20663876). Also catalyzes the reverse reactions, i.e. the isomerization of geraniol to linalool and the dehydration of linalool to myrcene (PubMed:20663876, PubMed:28068311, Ref.8). In this direction, the formation of myrcene from geraniol may be seen as a detoxification process for the monoterpene alcohol (PubMed:20663876). Shows a relatively broad substrate specificity and can use various geraniol and linalool derivatives (PubMed:28068311). Substrates required a specific alpha-methylallyl alcohol signature motif (PubMed:28068311). Neither the monoterpenes alpha- and beta-ocimene nor the monoterpenoids citronellol and nerol can be used as substrates (PubMed:20663876).<ref>PMID:20663876</ref> <ref>PMID:28068311</ref> [REFERENCE:8]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Castellaniella defragrans 65phen]]
+[[Category: Castellaniella defragrans 65Phen]]
 [[Category: Large Structures]]
-[[Category: Chambers, S]]
+[[Category: Chambers S]]
-[[Category: Grogan, G]]
+[[Category: Grogan G]]
-[[Category: Hau, A]]
+[[Category: Hau A]]
-[[Category: Man, H]]
+[[Category: Man H]]
-[[Category: Omar, M]]
+[[Category: Omar M]]
-[[Category: Turkenburg, J P]]
+[[Category: Turkenburg JP]]
-[[Category: Hydratase]]
-[[Category: Isomerase]]
-[[Category: Lyase]]
-[[Category: Terpene]]

5g1u

From Proteopedia

Current revision

Linalool Dehydratase Isomerase in complex with Geraniol

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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