6jfj | pdb_00006jfj

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

spinqualitylabelsall models 6jfj, resolution 1.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6jfj is a 1 chain structure with sequence from Paenibacillus barengoltzii. This structure supersedes the now removed PDB entry 5ww2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.932Å Ligands: 1PE, CA, CL, GLC, GOL, IMD, PEG, PGE, PRD_900009, PRD_900030, TAM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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