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==Crystal structure of Pullulanase from Paenibacillus barengoltzii complex with maltohexaose and alpha-cyclodextrin==
==Crystal structure of Pullulanase from Paenibacillus barengoltzii complex with maltohexaose and alpha-cyclodextrin==
<StructureSection load='6jfj' size='340' side='right' caption='[[6jfj]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
<StructureSection load='6jfj' size='340' side='right'caption='[[6jfj]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6jfj]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5ww2 5ww2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JFJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JFJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[6jfj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenibacillus_barengoltzii Paenibacillus barengoltzii]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5ww2 5ww2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JFJ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</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]] 1.932&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6jeq|6jeq]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PRD_900009:alpha-maltotriose'>PRD_900009</scene>, <scene name='pdbligand=PRD_900030:alpha-maltopentaose'>PRD_900030</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pullulanase Pullulanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.41 3.2.1.41] </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=6jfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jfj OCA], [https://pdbe.org/6jfj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jfj RCSB], [https://www.ebi.ac.uk/pdbsum/6jfj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jfj 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=6jfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jfj OCA], [http://pdbe.org/6jfj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jfj RCSB], [http://www.ebi.ac.uk/pdbsum/6jfj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jfj ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0C5GWS2_9BACL A0A0C5GWS2_9BACL]
<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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jfj" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Pullulanase]]
[[Category: Large Structures]]
[[Category: Huang, P]]
[[Category: Paenibacillus barengoltzii]]
[[Category: Jiang, Z Q]]
[[Category: Huang P]]
[[Category: Qin, Z]]
[[Category: Jiang ZQ]]
[[Category: Wu, S W]]
[[Category: Qin Z]]
[[Category: Yang, S Q]]
[[Category: Wu SW]]
[[Category: You, X]]
[[Category: Yang SQ]]
[[Category: Alpha-cyclodextrin]]
[[Category: You X]]
[[Category: Gh13]]
[[Category: Hydrolase]]
[[Category: Maltohexaose]]

Latest revision as of 10:08, 22 November 2023

Crystal structure of Pullulanase from Paenibacillus barengoltzii complex with maltohexaose and alpha-cyclodextrin

6jfj, resolution 1.93Å

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