5AH1

Structure of EstA from Clostridium botulinum

5AH1 の概要

• エントリーDOI: 10.2210/pdb5ah1/pdb
• 分子名称: TRIACYLGLYCEROL LIPASE, ZINC ION, POTASSIUM ION, ... (4 entities in total)
• 機能のキーワード: hydrolase, polyesterase, polymer hydrolysis, zinc binding, alpha/beta- hydrolase
• 由来する生物種: CLOSTRIDIUM BOTULINUM
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 51913.33

構造登録者

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. (登録日: 2015-02-04, 公開日: 2015-11-11, 最終更新日: 2024-01-10)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.2 Å)