6jr7: Difference between revisions
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<StructureSection load='6jr7' size='340' side='right'caption='[[6jr7]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='6jr7' size='340' side='right'caption='[[6jr7]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6jr7]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JR7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JR7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6jr7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Cytophaga_johnsonae Cytophaga johnsonae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JR7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JR7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6jr6|6jr6]], [[6jr8|6jr8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6jr6|6jr6]], [[6jr8|6jr8]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Fjoh_4430 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=376686 Cytophaga johnsonae])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-glucosidase Alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-glucosidase Alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20] </span></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=6jr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jr7 OCA], [http://pdbe.org/6jr7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jr7 RCSB], [http://www.ebi.ac.uk/pdbsum/6jr7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jr7 ProSAT]</span></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=6jr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jr7 OCA], [http://pdbe.org/6jr7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jr7 RCSB], [http://www.ebi.ac.uk/pdbsum/6jr7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jr7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<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> | |||
</div> | |||
<div class="pdbe-citations 6jr7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Alpha-glucosidase]] | [[Category: Alpha-glucosidase]] | ||
[[Category: Cytophaga johnsonae]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Tonozuka, T]] | [[Category: Tonozuka, T]] | ||
Revision as of 09:07, 10 October 2019
Flavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucoseFlavobacterium johnsoniae GH31 dextranase, FjDex31A, complexed with glucose
Structural highlights
Publication 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. References
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