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| | <StructureSection load='5a8d' size='340' side='right'caption='[[5a8d]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='5a8d' size='340' side='right'caption='[[5a8d]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5a8d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"ruminiclostridium_thermocellum"_(viljoen_et_al._1926)_yutin_and_galperin_2013 "ruminiclostridium thermocellum" (viljoen et al. 1926) yutin and galperin 2013]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A8D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A8D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5a8d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus Acetivibrio thermocellus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A8D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A8D 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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a8c|5a8c]]</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-reducing_end_alpha-L-arabinofuranosidase Non-reducing end alpha-L-arabinofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.55 3.2.1.55] </span></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=5a8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a8d OCA], [https://pdbe.org/5a8d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a8d RCSB], [https://www.ebi.ac.uk/pdbsum/5a8d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a8d 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=5a8d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a8d OCA], [http://pdbe.org/5a8d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a8d RCSB], [http://www.ebi.ac.uk/pdbsum/5a8d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a8d ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A3DEX4_ACET2 A3DEX4_ACET2] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Acetivibrio thermocellus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Non-reducing end alpha-L-arabinofuranosidase]]
| + | [[Category: Ahmed S]] |
| - | [[Category: Ahmed, S]] | + | [[Category: Fontes CMGA]] |
| - | [[Category: Fontes, C M.G A]] | + | [[Category: Goyal A]] |
| - | [[Category: Goyal, A]] | + | [[Category: Najmudin S]] |
| - | [[Category: Najmudin, S]] | + | [[Category: Sharma K]] |
| - | [[Category: Sharma, K]] | + | |
| - | [[Category: 5-fold-beta-propeller]]
| + | |
| - | [[Category: Alpha-l-arabinofuranosidase]]
| + | |
| - | [[Category: C. thermocellum]]
| + | |
| - | [[Category: Ctgh43]]
| + | |
| - | [[Category: Glycoside hydrolase]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
A3DEX4_ACET2
Publication Abstract from PubMed
The recent division of the large glycoside hydrolase family 43 (GH43) into subfamilies offers a renewed opportunity to develop structure-function studies aimed at clarifying the molecular determinants of substrate specificity in carbohydrate-degrading enzymes. alpha-L-Arabinofuranosidases (EC 3.2.1.55) remove arabinose side chains from heteropolysaccharides such as xylan and arabinan. However, there is some evidence suggesting that arabinofuranosidases are substrate-specific, being unable to display a debranching activity on different polysaccharides. Here, the structure of Clostridium thermocellum arabinofuranosidase 43A (CtAbf43A), which has been shown to act in the removal of arabinose side chains from arabinoxylan but not from pectic arabinan, is reported. CtAbf43A belongs to GH43 subfamily 16, the members of which have a restricted capacity to attack xylans. The crystal structure of CtAbf43A comprises a five-bladed beta-propeller fold typical of GH43 enzymes. CtAbf43A displays a highly compact architecture compatible with its high thermostability. Analysis of CtAbf43A along with the other member of GH43 subfamily 16 with known structure, the Bacillus subtilis arabinofuranosidase BsAXH-m2,3, suggests that the specificity of subfamily 16 for arabinoxylan is conferred by a long surface substrate-binding cleft that is complementary to the xylan backbone. The lack of a curved-shaped carbohydrate-interacting platform precludes GH43 subfamily 16 enzymes from interacting with the nonlinear arabinan scaffold and therefore from deconstructing this polysaccharide.
Molecular determinants of substrate specificity revealed by the structure of Clostridium thermocellum arabinofuranosidase 43A from glycosyl hydrolase family 43 subfamily 16.,Goyal A, Ahmed S, Sharma K, Gupta V, Bule P, Alves VD, Fontes CM, Najmudin S Acta Crystallogr D Struct Biol. 2016 Dec 1;72(Pt 12):1281-1289. Epub 2016 Nov 29. PMID:27917828[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Goyal A, Ahmed S, Sharma K, Gupta V, Bule P, Alves VD, Fontes CM, Najmudin S. Molecular determinants of substrate specificity revealed by the structure of Clostridium thermocellum arabinofuranosidase 43A from glycosyl hydrolase family 43 subfamily 16. Acta Crystallogr D Struct Biol. 2016 Dec 1;72(Pt 12):1281-1289. Epub 2016 Nov 29. PMID:27917828 doi:http://dx.doi.org/10.1107/S205979831601737X
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