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| | <StructureSection load='6jhf' size='340' side='right'caption='[[6jhf]], [[Resolution|resolution]] 1.71Å' scene=''> | | <StructureSection load='6jhf' size='340' side='right'caption='[[6jhf]], [[Resolution|resolution]] 1.71Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6jhf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_baa-1209 Atcc baa-1209]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5wvq 5wvq]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JHF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6JHF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6jhf]] 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=5wvq 5wvq]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JHF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 1.71Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6jeq|6jeq]], [[6jfj|6jfj]], [[6jfx|6jfx]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=6jhf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jhf OCA], [https://pdbe.org/6jhf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jhf RCSB], [https://www.ebi.ac.uk/pdbsum/6jhf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jhf 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=6jhf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jhf OCA], [http://pdbe.org/6jhf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jhf RCSB], [http://www.ebi.ac.uk/pdbsum/6jhf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jhf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0C5GWS2_9BACL A0A0C5GWS2_9BACL] |
| | <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: Atcc baa-1209]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pullulanase]] | + | [[Category: Paenibacillus barengoltzii]] |
| - | [[Category: Huang, P]] | + | [[Category: Huang P]] |
| - | [[Category: Jiang, Z Q]] | + | [[Category: Jiang ZQ]] |
| - | [[Category: Qin, Z]] | + | [[Category: Qin Z]] |
| - | [[Category: Wu, S W]] | + | [[Category: Wu SW]] |
| - | [[Category: Yang, S Q]] | + | [[Category: Yang SQ]] |
| - | [[Category: You, X]] | + | [[Category: You X]] |
| - | [[Category: Gh13]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
A0A0C5GWS2_9BACL
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Huang P, Wu S, Yang S, Yan Q, Jiang Z. Structural basis of carbohydrate binding in domain C of a type I pullulanase from Paenibacillus barengoltzii. Acta Crystallogr D Struct Biol. 2020 May 1;76(Pt 5):447-457. doi:, 10.1107/S205979832000409X. Epub 2020 Apr 23. PMID:32355041 doi:http://dx.doi.org/10.1107/S205979832000409X
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