research papers
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.
Supporting information
Portable Document Format (PDF) file https://doi.org/10.1107/S2059798319010660/jc5025sup1.pdf |
PDB references: PulA from Klebsiella pneumoniae, ligand-free, 6j33; maltotriose complex, 6j34; G680L mutant, ligand-free, 6j35; G680L mutant, maltotriose complex, 6j4h