6jfx
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6jfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jfx OCA], [http://pdbe.org/6jfx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jfx RCSB], [http://www.ebi.ac.uk/pdbsum/6jfx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jfx ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6jfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jfx OCA], [http://pdbe.org/6jfx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jfx RCSB], [http://www.ebi.ac.uk/pdbsum/6jfx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jfx ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pullulanase (EC 3.2.1.41) is a well known starch-debranching enzyme that catalyzes the cleavage of alpha-1,6-glycosidic linkages in alpha-glucans such as starch and pullulan. Crystal structures of a type I pullulanase from Paenibacillus barengoltzii (PbPulA) and of PbPulA in complex with maltopentaose (G5), maltohexaose (G6)/alpha-cyclodextrin (alpha-CD) and beta-cyclodextrin (beta-CD) were determined in order to better understand substrate binding to this enzyme. PbPulA belongs to glycoside hydrolase (GH) family 13 subfamily 14 and is composed of three domains (CBM48, A and C). Three carbohydrate-binding sites identified in PbPulA were located in CBM48, near the active site and in domain C, respectively. The binding site in CBM48 was specific for beta-CD, while that in domain C has not been reported for other pullulanases. The domain C binding site had higher affinity for alpha-CD than for G6; a small motif (FGGEH) seemed to be one of the major determinants for carbohydrate binding in this domain. Structure-based mutations of several surface-exposed aromatic residues in CBM48 and domain C had a debilitating effect on the activity of the enzyme. These results suggest that both CBM48 and domain C play a role in binding substrates. The crystal forms described contribute to the understanding of pullulanase domain-carbohydrate interactions. | ||
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| + | Structural basis of carbohydrate binding in domain C of a type I pullulanase from Paenibacillus barengoltzii.,Huang P, Wu S, Yang S, Yan Q, Jiang Z Acta Crystallogr D Struct Biol. 2020 May 1;76(Pt 5):447-457. doi:, 10.1107/S205979832000409X. Epub 2020 Apr 23. PMID:32355041<ref>PMID:32355041</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6jfx" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 05:44, 13 May 2020
Crystal structure of Pullulanase from Paenibacillus barengoltzii complex with maltopentaose
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Categories: Atcc baa-1209 | Large Structures | Pullulanase | Huang, P | Jiang, Z Q | Qin, Z | Wu, S W | Yang, S Q | You, X | Gh13 | Hydrolase | Maltopentaose
