6k1g
From Proteopedia
(Difference between revisions)
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==Crystal structure of the L-fucose isomerase soaked with Mn2+ from Raoultella sp.== | ==Crystal structure of the L-fucose isomerase soaked with Mn2+ from Raoultella sp.== | ||
- | <StructureSection load='6k1g' size='340' side='right'caption='[[6k1g]]' scene=''> | + | <StructureSection load='6k1g' size='340' side='right'caption='[[6k1g]], [[Resolution|resolution]] 2.96Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K1G OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6K1G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6k1g]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33531 Atcc 33531]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K1G OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6K1G FirstGlance]. <br> |
- | </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=6k1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k1g OCA], [http://pdbe.org/6k1g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k1g RCSB], [http://www.ebi.ac.uk/pdbsum/6k1g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k1g ProSAT]</span></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> |
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fucI, NCTC13095_01108 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=575 ATCC 33531])</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-fucose_isomerase L-fucose isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.25 5.3.1.25] </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=6k1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k1g OCA], [http://pdbe.org/6k1g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k1g RCSB], [http://www.ebi.ac.uk/pdbsum/6k1g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k1g ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Background: l-Fucose is a rare sugar with potential uses in the pharmaceutical, cosmetic, and food industries. The enzymatic approach using l-fucose isomerase, which interconverts l-fucose and l-fuculose, can be an efficient way of producing l-fucose for industrial applications. Here, we performed biochemical and structural analyses of l-fucose isomerase identified from a novel species of Raoultella (RdFucI). Results: RdFucI exhibited higher enzymatic activity for l-fuculose than for l-fucose, and the rate for the reverse reaction of converting l-fuculose to l-fucose was higher than that for the forward reaction of converting l-fucose to l-fuculose. In the equilibrium mixture, a much higher proportion of l-fucose (~ ninefold) was achieved at 30 degrees C and pH 7, indicating that the enzyme-catalyzed reaction favors the formation of l-fucose from l-fuculose. When biochemical analysis was conducted using l-fuculose as the substrate, the optimal conditions for RdFucI activity were determined to be 40 degrees C and pH 10. However, the equilibrium composition was not affected by reaction temperature in the range of 30 to 50 degrees C. Furthermore, RdFucI was found to be a metalloenzyme requiring Mn(2+) as a cofactor. The comparative crystal structural analysis of RdFucI revealed the distinct conformation of alpha7-alpha8 loop of RdFucI. The loop is present at the entry of the substrate binding pocket and may affect the catalytic activity. Conclusions: RdFucI-catalyzed isomerization favored the reaction from l-fuculose to l-fucose. The biochemical and structural data of RdFucI will be helpful for the better understanding of the molecular mechanism of l-FucIs and the industrial production of l-fucose. | ||
+ | |||
+ | Enzymatic synthesis of l-fucose from l-fuculose using a fucose isomerase from Raoultella sp. and the biochemical and structural analyses of the enzyme.,Kim IJ, Kim DH, Nam KH, Kim KH Biotechnol Biofuels. 2019 Dec 5;12:282. doi: 10.1186/s13068-019-1619-0., eCollection 2019. PMID:31827610<ref>PMID:31827610</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6k1g" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Atcc 33531]] | ||
+ | [[Category: L-fucose isomerase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Kim | + | [[Category: Kim, D H]] |
- | [[Category: Kim | + | [[Category: Kim, I J]] |
- | [[Category: Kim | + | [[Category: Kim, K H]] |
- | [[Category: Nam | + | [[Category: Nam, K H]] |
+ | [[Category: Fucose]] | ||
+ | [[Category: Isomerase]] |
Revision as of 11:21, 29 July 2020
Crystal structure of the L-fucose isomerase soaked with Mn2+ from Raoultella sp.
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Categories: Atcc 33531 | L-fucose isomerase | Large Structures | Kim, D H | Kim, I J | Kim, K H | Nam, K H | Fucose | Isomerase