4ttu: Difference between revisions
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==N-terminally truncated dextransucrase DSR-E from Leuconostoc mesenteroides NRRL B-1299 in complex with isomaltotriose== | ==N-terminally truncated dextransucrase DSR-E from Leuconostoc mesenteroides NRRL B-1299 in complex with isomaltotriose== | ||
<StructureSection load='4ttu' size='340' side='right' caption='[[4ttu]], [[Resolution|resolution]] 2.18Å' scene=''> | <StructureSection load='4ttu' size='340' side='right'caption='[[4ttu]], [[Resolution|resolution]] 2.18Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ttu]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TTU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TTU FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ttu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"ascococcus_mesenteroides"_tsenkovskii_1878 "ascococcus mesenteroides" tsenkovskii 1878]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TTU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TTU FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IYR:3-IODO-TYROSINE'>IYR</scene>, <scene name='pdbligand=TYI:3,5-DIIODOTYROSINE'>TYI</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IYR:3-IODO-TYROSINE'>IYR</scene>, <scene name='pdbligand=TYI:3,5-DIIODOTYROSINE'>TYI</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ttq|3ttq]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ttq|3ttq]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dsrE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1245 "Ascococcus mesenteroides" Tsenkovskii 1878])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dextransucrase Dextransucrase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.5 2.4.1.5] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dextransucrase Dextransucrase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.5 2.4.1.5] </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=4ttu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ttu OCA], [http://pdbe.org/4ttu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ttu RCSB], [http://www.ebi.ac.uk/pdbsum/4ttu PDBsum]</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=4ttu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ttu OCA], [http://pdbe.org/4ttu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ttu RCSB], [http://www.ebi.ac.uk/pdbsum/4ttu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ttu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ascococcus mesenteroides tsenkovskii 1878]] | |||
[[Category: Dextransucrase]] | [[Category: Dextransucrase]] | ||
[[Category: Large Structures]] | |||
[[Category: Brison, Y]] | [[Category: Brison, Y]] | ||
[[Category: Mourey, L]] | [[Category: Mourey, L]] |
Revision as of 17:57, 10 May 2019
N-terminally truncated dextransucrase DSR-E from Leuconostoc mesenteroides NRRL B-1299 in complex with isomaltotrioseN-terminally truncated dextransucrase DSR-E from Leuconostoc mesenteroides NRRL B-1299 in complex with isomaltotriose
Structural highlights
Publication Abstract from PubMedThe alpha-(1-->2) branching sucrase DeltaN123-GBD-CD2 is an enzyme belonging to the Glycoside-Hydrolase family 70 (GH70) that catalyses the transfer of D-glucosyl units from sucrose to dextrans or glucooligosaccharides via the formation of alpha-(1-->2) glucosidic linkages. The first structures of DeltaN123-GBD-CD2 in complex with D-glucose, isomaltosyl or isomaltotriosyl residues were solved. The glucose complex revealed three glucose binding sites in the catalytic gorge and six additional ones at the surface of domains B, IV and V. Soaking with isomaltotriose or glucooligosaccharides led to structures in which isomaltosyl or isomaltriosyl residues were found in glucan binding pockets belonging to domain V. One aromatic residue is systematically identified at the bottom of these pockets in stacking interaction with one glucosyl moiety. The carbohydrate is also maintained by a network of hydrogen bonds and van der Waals interactions. The sequence of these binding pockets is conserved and repeatedly present in the domain V of GH70 glucansucrases known to bind alpha-glucans. These findings provide the first structural evidence of the molecular interaction occurring between isomaltooligosaccharides and the domain V of the GH70 enzymes. Structural insights into the carbohydrate-binding ability of an alpha-(1-->2) branching sucrase from glycoside-hydrolase family 70.,Brison Y, Malbert Y, Czaplicki G, Mourey L, Remaud-Simeon M, Tranier S J Biol Chem. 2016 Feb 10. pii: jbc.M115.688796. PMID:26865636[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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