4bzz | pdb_00004bzz

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

spinqualitylabelsall models 4bzz, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4bzz is a 1 chain structure with sequence from Lactiplantibacillus plantarum WCFS1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3Å Ligands: ACT, CCN, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function F9US10_LACPL Publication Abstract from PubMed The alpha/beta 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. Here, we report the crystal structure of the carboxylesterase Cest-2923 from the lactic acid bacterium Lactobacillus plantarum WCFS1 refined to 2.1 A 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 alpha/beta-hydrolase fold, the basic framework of the crystal structure of Cest-2923, also extends to its oligomeric behavior in solution. Thus, we discovered that Cest-2923 exhibits a pH-dependent pleomorphic behaviour in solution involving monomers, canonical dimers and tetramers. Whereas at neutral pH the system is mainly shifted to dimeric species, at acidic conditions tetrameric species predominate. Interestingly, despite that these tetramers result from the association of canonical dimers, as commonly found in many other carboxylesterases from the hormone-sensitive lipase family, they can be defined as "non canonical" since they represent a different association mode. We identified this same type of tetramers in the closest relative of Cest-2923 structurally characterized, the sugar hydrolase YeeB from Lactococcus lactis. Interestingly, the observed associative behaviour is consistent with different crystallographic results of Cest-2923 from structural genomics consortia. Finally, we benefit from the presence of sulphate or acetate molecules (depending on the crystal form analysed) in the close vicinity of the nucleophile Ser116, to identify interactions with the putative oxyanion hole and also to deduce the existence of hydrolytic activity within Cest-2923 crystals. This article is protected by copyright. All rights reserved. Structure, biochemical characterization and analysis of the pleomorphism of carboxylesterase Cest-2923 from Lactobacillus plantarum WCFS1.,Benavente R, Esteban-Torres M, Acebron I, de Las Rivas B, Munoz R, Alvarez Y, Mancheno JM FEBS J. 2013 Oct 16. doi: 10.1111/febs.12569. PMID:24127688 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lipase 3D Structures

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