4BZZ

Complete crystal structure of carboxylesterase Cest-2923 from Lactobacillus plantarum WCFS1

4BZZ の概要

• エントリーDOI: 10.2210/pdb4bzz/pdb
• 関連するPDBエントリー: 4BZW 4C01
• 分子名称: LIPASE/ESTERASE, ACETATE ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: hydrolase, carboxylesterase
• 由来する生物種: LACTOBACILLUS PLANTARUM
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31877.74

構造登録者

Benavente, R.,Esteban-Torres, M.,Acebron, I.,de las Rivas, B.,Munoz, R.,Alvarez, Y.,Mancheno, J.M. (登録日: 2013-07-30, 公開日: 2013-10-30, 最終更新日: 2023-12-20)

主引用文献

Benavente, R.,Esteban-Torres, M.,Acebron, I.,De Las Rivas, B.,Munoz, R.,Alvarez, Y.,Mancheno, J.M.
Structure, Biochemical Characterization and Analysis of the Pleomorphism of Carboxylesterase Cest-2923 from Lactobacillus Plantarum Wcfs1
FEBS J., 280:6658-, 2013

PubMed Abstract: The hydrolase fold is one of the most versatile structures in the protein realm according to the diversity of sequences adopting such a three-dimensional architecture. In the present study, we clarified the crystal structure of the carboxylesterase Cest-2923 from the lactic acid bacterium Lactobacillus plantarum WCFS1 refined to 2.1 Å resolution, determined its main biochemical characteristics and also carried out an analysis of its associative behaviour in solution. We found that the versatility of a canonical α/β hydrolase fold, the basic framework of the crystal structure of Cest-2923, also extends to its oligomeric behaviour in solution. Thus, we discovered that Cest-2923 exhibits a pH-dependent pleomorphic behaviour in solution involving monomers, canonical dimers and tetramers. Although, at neutral pH, the system is mainly shifted to dimeric species, under acidic conditions, tetrameric species predominate. Despite these tetramers resulting from the association of canonical dimers, as is commonly found in many other carboxylesterases from the hormone-sensitive lipase family, they can be defined as 'noncanonical' because they represent a different association mode. We identified this same type of tetramer in the closest relative of Cest-2923 that has been structurally characterized: the sugar hydrolase YeeB from Lactococcus lactis. The observed associative behaviour is consistent with the different crystallographic results for Cest-2923 from structural genomics consortia. Finally, the presence of sulfate or acetate molecules (depending on the crystal form analysed) in the close vicinity of the nucleophile Ser116 allows us to identify interactions with the putative oxyanion hole and deduce the existence of hydrolytic activity within Cest-2923 crystals.

PubMed: 24127688
DOI: 10.1111/FEBS.12569

実験手法

X-RAY DIFFRACTION (3 Å)