6J33

Crystal structure of ligand-free of PulA from Klebsiella pneumoniae

Summary for 6J33

• Entry DOI: 10.2210/pdb6j33/pdb
• Descriptor: pullulanase, MAGNESIUM ION, ACETATE ION, ... (5 entities in total)
• Functional Keywords: pullulanase, klebsiella pneumoniae, ligand-free, g680, hydrolase
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 2
• Total formula weight: 229972.56

Authors

Saka, N.,Iwamoto, H.,Takahashi, N.,Mizutani, K.,Mikami, B. (deposition date: 2019-01-09, release date: 2019-09-18, Last modification date: 2024-10-23)

Primary citation

Saka, N.,Malle, D.,Iwamoto, H.,Takahashi, N.,Mizutani, K.,Mikami, B.
Relationship between the induced-fit loop and the activity of Klebsiella pneumoniae pullulanase.
Acta Crystallogr D Struct Biol, 75:792-803, 2019

PubMed Abstract: 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.

PubMed: 31478902
DOI: 10.1107/S2059798319010660

Experimental method

X-RAY DIFFRACTION (1.297 Å)