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6k1f

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==Crystal structure of the L-fucose isomerase from Raoultella sp.==
==Crystal structure of the L-fucose isomerase from Raoultella sp.==
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<StructureSection load='6k1f' size='340' side='right'caption='[[6k1f]]' scene=''>
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<StructureSection load='6k1f' size='340' side='right'caption='[[6k1f]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6K1F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6K1F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6k1f]] 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=6K1F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6K1F FirstGlance]. <br>
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</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=6k1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k1f OCA], [http://pdbe.org/6k1f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k1f RCSB], [http://www.ebi.ac.uk/pdbsum/6k1f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k1f ProSAT]</span></td></tr>
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</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>
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<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>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6k1f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6k1f OCA], [http://pdbe.org/6k1f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6k1f RCSB], [http://www.ebi.ac.uk/pdbsum/6k1f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6k1f ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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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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<div class="pdbe-citations 6k1f" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 33531]]
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[[Category: L-fucose isomerase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Kim DH]]
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[[Category: Kim, D H]]
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[[Category: Kim IJ]]
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[[Category: Kim, I J]]
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[[Category: Kim KH]]
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[[Category: Kim, K H]]
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[[Category: Nam KH]]
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[[Category: Nam, K H]]
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[[Category: Fucose]]
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[[Category: Isomerase]]

Revision as of 11:21, 29 July 2020

Crystal structure of the L-fucose isomerase from Raoultella sp.

PDB ID 6k1f

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