6a8i
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of endo-arabinanase ABN-TS D147N mutant in complex with arabinohexaose== | |
| + | <StructureSection load='6a8i' size='340' side='right' caption='[[6a8i]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6a8i]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A8I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A8I FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AHR:ALPHA-L-ARABINOFURANOSE'>AHR</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arabinan_endo-1,5-alpha-L-arabinosidase Arabinan endo-1,5-alpha-L-arabinosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.99 3.2.1.99] </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=6a8i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a8i OCA], [http://pdbe.org/6a8i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a8i RCSB], [http://www.ebi.ac.uk/pdbsum/6a8i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a8i ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/IABN_GEOTD IABN_GEOTD]] Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of endo alpha-(1->5)-L-arabinofuranosyl residues in debranched arabinan.<ref>PMID:11999422</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The thermostable endo-1,5-alpha-L-arabinanase from Bacillus thermodenitrificans TS-3 (ABN-TS) hydrolyzes the alpha-1,5-L-arabinofuranoside linkages of arabinan. In this study, the crystal structures of inactive ABN-TS mutants, D27A and D147N, were determined in complex with arabino-oligosaccharides. The crystal structures revealed that ABN-TS has at least six subsites in the deep V-shaped cleft formed across one face of the propeller structure. The structural features indicate that substrate recognition is profoundly influenced by the remote subsites as well as by the subsites surrounding the active center. The `open' structure of the substrate-binding cleft of the endo-acting ABN-TS is suitable for the random binding of several sugar units in polymeric substrates. | ||
| - | + | Structures of endo-1,5-alpha-L-arabinanase mutants from Bacillus thermodenitrificans TS-3 in complex with arabino-oligosaccharides.,Yamaguchi A, Sogabe Y, Fukuoka S, Sakai T, Tada T Acta Crystallogr F Struct Biol Commun. 2018 Dec 1;74(Pt 12):774-780. doi:, 10.1107/S2053230X18015947. Epub 2018 Nov 26. PMID:30511671<ref>PMID:30511671</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 6a8i" style="background-color:#fffaf0;"></div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arabinan endo-1,5-alpha-L-arabinosidase]] | ||
[[Category: Tada, T]] | [[Category: Tada, T]] | ||
| + | [[Category: Yamaguchi, A]] | ||
| + | [[Category: Arabinanase]] | ||
| + | [[Category: Gh43]] | ||
| + | [[Category: Glycoside hydrolase]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Thermostable enzyme]] | ||
Revision as of 08:15, 19 December 2018
Crystal structure of endo-arabinanase ABN-TS D147N mutant in complex with arabinohexaose
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