6j35

Crystal structure of ligand-free of PulA-G680L mutant from Klebsiella pneumoniae

spinqualitylabelsall models 6j35, resolution 1.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6j35 is a 2 chain structure with sequence from Klebsiella pneumoniae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.839Å Ligands: CA, GOL, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function W9BQ28_KLEPN Publication Abstract from PubMed Klebsiella pneumoniae pullulanase (KPP) belongs to glycoside hydrolase family 13 subfamily 13 (GH13_13) and is the only enzyme that is reported to perform an induced-fit motion of the active-site loop (residues 706-710). Comparison of pullulanase structures indicated that only KPP has Leu680 present behind the loop, in contrast to the glycine found in other GH13_13 members. Analysis of the structure and activity of recombinant pullulanase from K. pneumoniae ATCC 9621 (rKPP) and its mutant (rKPP-G680L) indicated that the side chain of residue 680 is important for the induced-fit motion of the loop 706-710 and alters the binding affinity of the substrate. Relationship between the induced-fit loop and the activity of Klebsiella pneumoniae pullulanase.,Saka N, Malle D, Iwamoto H, Takahashi N, Mizutani K, Mikami B Acta Crystallogr D Struct Biol. 2019 Sep 1;75(Pt 9):792-803. doi: , 10.1107/S2059798319010660. Epub 2019 Aug 22. PMID:31478902 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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