6jr6: Difference between revisions
New page: '''Unreleased structure''' The entry 6jr6 is ON HOLD Authors: Tonozuka, T. Description: Flavobacterium johnsoniae GH31 dextranase, FjDex31A Category: Unreleased Structures [[Catego... |
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The | ==Flavobacterium johnsoniae GH31 dextranase, FjDex31A== | ||
<StructureSection load='6jr6' size='340' side='right'caption='[[6jr6]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6jr6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Flavobacterium_johnsoniae_UW101 Flavobacterium johnsoniae UW101]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JR6 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></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=6jr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jr6 OCA], [https://pdbe.org/6jr6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jr6 RCSB], [https://www.ebi.ac.uk/pdbsum/6jr6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jr6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A5FBI1_FLAJ1 A5FBI1_FLAJ1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Glycoside hydrolase family (GH) 31 contains a large variety of enzymes, but the major members are enzymes that act on relatively small oligosaccharides such as alpha-glucosidase. Here, we determined the crystal structure of FjDex31A, an enzyme from Flavobacterium johnsoniae that hydrolyzes a polysaccharide, dextran. FjDex31A is composed of four domains: an N-terminal domain, a catalytic domain, a proximal C-terminal domain, and a distal C-terminal domain, as observed in typical GH31 enzymes. However, the architecture of active site residues in FjDex31A, other than subsite -1, is markedly different from that of other GH31 enzymes. The FjDex31A structure in complex with isomaltotriose shows that Gly273 and Tyr524, both of which interact with an alpha-glucose residue at subsite -2, as well as Trp376 and Leu308-cisGln309, are especially unique to FjDex31A. Site-directed mutagenesis of Gly273 and Tyr524 resulted in a decrease in the hydrolysis of polysaccharides dextran and pullulan, as well as that of the disaccharide isomaltose. These results suggest that, regardless of the length of sugar chains of the substrates, binding of FjDex31A to the substrates at subsite -2 is likely to be important for its activity. | |||
Structural insights into polysaccharide recognition by Flavobacterium johnsoniae dextranase, a member of glycoside hydrolase family 31.,Tsutsumi K, Gozu Y, Nishikawa A, Tonozuka T FEBS J. 2019 Sep 25. doi: 10.1111/febs.15074. PMID:31552702<ref>PMID:31552702</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Tonozuka | <div class="pdbe-citations 6jr6" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Flavobacterium johnsoniae UW101]] | |||
[[Category: Large Structures]] | |||
[[Category: Tonozuka T]] | |||
Latest revision as of 13:07, 23 October 2024
Flavobacterium johnsoniae GH31 dextranase, FjDex31AFlavobacterium johnsoniae GH31 dextranase, FjDex31A
Structural highlights
FunctionPublication Abstract from PubMedGlycoside hydrolase family (GH) 31 contains a large variety of enzymes, but the major members are enzymes that act on relatively small oligosaccharides such as alpha-glucosidase. Here, we determined the crystal structure of FjDex31A, an enzyme from Flavobacterium johnsoniae that hydrolyzes a polysaccharide, dextran. FjDex31A is composed of four domains: an N-terminal domain, a catalytic domain, a proximal C-terminal domain, and a distal C-terminal domain, as observed in typical GH31 enzymes. However, the architecture of active site residues in FjDex31A, other than subsite -1, is markedly different from that of other GH31 enzymes. The FjDex31A structure in complex with isomaltotriose shows that Gly273 and Tyr524, both of which interact with an alpha-glucose residue at subsite -2, as well as Trp376 and Leu308-cisGln309, are especially unique to FjDex31A. Site-directed mutagenesis of Gly273 and Tyr524 resulted in a decrease in the hydrolysis of polysaccharides dextran and pullulan, as well as that of the disaccharide isomaltose. These results suggest that, regardless of the length of sugar chains of the substrates, binding of FjDex31A to the substrates at subsite -2 is likely to be important for its activity. Structural insights into polysaccharide recognition by Flavobacterium johnsoniae dextranase, a member of glycoside hydrolase family 31.,Tsutsumi K, Gozu Y, Nishikawa A, Tonozuka T FEBS J. 2019 Sep 25. doi: 10.1111/febs.15074. PMID:31552702[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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