5AH1

Structure of EstA from Clostridium botulinum

Summary for 5AH1

• Entry DOI: 10.2210/pdb5ah1/pdb
• Descriptor: TRIACYLGLYCEROL LIPASE, ZINC ION, POTASSIUM ION, ... (4 entities in total)
• Functional Keywords: hydrolase, polyesterase, polymer hydrolysis, zinc binding, alpha/beta- hydrolase
• Biological source: CLOSTRIDIUM BOTULINUM
• Total number of polymer chains: 1
• Total formula weight: 51913.33

Authors

Pairitsch, A.,Lyskowski, A.,Hromic, A.,Steinkellner, G.,Gruber, K.,Perz, V.,Baumschlager, A.,Bleymaier, K.,Zitzenbacher, S.,Sinkel, C.,Kueper, U.,Ribitsch, D.,Guebitz, G.M. (deposition date: 2015-02-04, release date: 2015-11-11, Last modification date: 2024-01-10)

Primary citation

Perz, V.,Baumschlager, A.,Bleymaier, K.,Zitzenbacher, S.,Hromic, A.,Steinkellner, G.,Pairitsch, A.,Lyskowski, A.,Gruber, K.,Sinkel, C.,Kueper, U.,Ribitsch, D.,Guebitz, G.M.
Hydrolysis of Synthetic Polyesters by Clostridium Botulinum Esterases.
Biotechnol.Bioeng., 113:1024-, 2016

PubMed Abstract: Two novel esterases from the anaerobe Clostridium botulinum ATCC 3502 (Cbotu_EstA and Cbotu_EstB) were expressed in Escherichia coli BL21-Gold(DE3) and were found to hydrolyze the polyester poly(butylene adipate-co-butylene terephthalate) (PBAT). The active site residues (triad Ser, Asp, His) are present in both enzymes at the same location only with some amino acid variations near the active site at the surrounding of aspartate. Yet, Cbotu_EstA showed higher kcat values on para-nitrophenyl butyrate and para-nitrophenyl acetate and was considerably more active (sixfold) on PBAT. The entrance to the active site of the modeled Cbotu_EstB appears more narrowed compared to the crystal structure of Cbotu_EstA and the N-terminus is shorter which could explain its lower activity on PBAT. The Cbotu_EstA crystal structure consists of two regions that may act as movable cap domains and a zinc metal binding site.

PubMed: 26524601
DOI: 10.1002/BIT.25874

Experimental method

X-RAY DIFFRACTION (1.2 Å)