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''' | ==Crystal Structure of gamma-carotenoid desaturase== | ||
<StructureSection load='4rep' size='340' side='right' caption='[[4rep]], [[Resolution|resolution]] 1.97Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4rep]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4REP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4REP FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rep FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rep OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rep RCSB], [http://www.ebi.ac.uk/pdbsum/4rep PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The gamma-carotenoids, such as myxol and saproxanthin, have a high potential to be utilized in nutraceutical and pharmaceutical industries for their neuro-protective and antioxidant effects. CrtD is involved in the production of gamma-carotenoids by desaturating the C3'-C4' position of 1'-OH-gamma-carotenoid. We determined the crystal structure of CrtD from Nonlabens dokdonensis DSW-6 (NdCrtD), the first structure of CrtD family enzymes. The NdCrtD structure was composed of two distinct domains, an FAD-binding domain and a substrate-binding domain, and the substrate-binding domain can be divided into two subdomains, a Rossmann fold-like subdomain and a lid subdomain. Although the FAD-binding domain showed a structure similar to canonical FAD-containing enzymes, the substrate-binding domain exhibited a novel structure to constitute a long and hydrophobic tunnel with a length of approximately 40A. The molecular docking-simulation reveals that the tunnel provides an appropriate substrate-binding site for the carotenoid such as 1'-OH-gamma-carotene with a length of approximately 35A. We could predict residues related to recognize the 1'-hydroxyl group and to stabilize the hydrophobic end without hydroxyl group. Moreover, we suggest that the flexible entrance loop may undergo an open-closed formational change during the binding of the substrate. | |||
Crystal structure of 1'-OH-carotenoid 3,4-desaturase from Nonlabens dokdonensis DSW-6.,Ahn JW, Kim KJ Enzyme Microb Technol. 2015 Sep;77:29-37. doi: 10.1016/j.enzmictec.2015.05.005., Epub 2015 May 22. PMID:26138397<ref>PMID:26138397</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
[[Category: | <references/> | ||
[[Category: Kim, K | __TOC__ | ||
</StructureSection> | |||
[[Category: Ahn, J W]] | |||
[[Category: Kim, E J]] | |||
[[Category: Kim, K J]] | |||
[[Category: Kim, S]] | [[Category: Kim, S]] | ||
[[Category: | [[Category: Desaturase]] | ||
[[Category: | [[Category: Fad-binding]] | ||
[[Category: Flavoprotein]] | |||
[[Category: Gamma-carotenoid desaturase]] | |||
[[Category: Oxidoreductase]] | |||
[[Category: Rossmann fold]] | |||
Revision as of 16:27, 15 July 2015
Crystal Structure of gamma-carotenoid desaturaseCrystal Structure of gamma-carotenoid desaturase
Structural highlights
Publication Abstract from PubMedThe gamma-carotenoids, such as myxol and saproxanthin, have a high potential to be utilized in nutraceutical and pharmaceutical industries for their neuro-protective and antioxidant effects. CrtD is involved in the production of gamma-carotenoids by desaturating the C3'-C4' position of 1'-OH-gamma-carotenoid. We determined the crystal structure of CrtD from Nonlabens dokdonensis DSW-6 (NdCrtD), the first structure of CrtD family enzymes. The NdCrtD structure was composed of two distinct domains, an FAD-binding domain and a substrate-binding domain, and the substrate-binding domain can be divided into two subdomains, a Rossmann fold-like subdomain and a lid subdomain. Although the FAD-binding domain showed a structure similar to canonical FAD-containing enzymes, the substrate-binding domain exhibited a novel structure to constitute a long and hydrophobic tunnel with a length of approximately 40A. The molecular docking-simulation reveals that the tunnel provides an appropriate substrate-binding site for the carotenoid such as 1'-OH-gamma-carotene with a length of approximately 35A. We could predict residues related to recognize the 1'-hydroxyl group and to stabilize the hydrophobic end without hydroxyl group. Moreover, we suggest that the flexible entrance loop may undergo an open-closed formational change during the binding of the substrate. Crystal structure of 1'-OH-carotenoid 3,4-desaturase from Nonlabens dokdonensis DSW-6.,Ahn JW, Kim KJ Enzyme Microb Technol. 2015 Sep;77:29-37. doi: 10.1016/j.enzmictec.2015.05.005., Epub 2015 May 22. PMID:26138397[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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