8axc

Crystal structure of mouse Ces2c

spinqualitylabelsall models 8axc, resolution 2.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8axc is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.12Å Ligands: CL, NCA, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EST2C_MOUSE Hydrolase with high activity towards palmitoylcarnitine. Is also active with p-nitrophenylacetate and alpha-naphthylacetate. May also hydrolyze retinyl esters (By similarity).[UniProtKB:O70631] Publication Abstract from PubMed Members of the carboxylesterase 2 (Ces2/CES2) family have been studied intensively with respect to their hydrolytic function on (pro)drugs, whereas their physiological role in lipid and energy metabolism has been realized only within the last few years. Humans have one CES2 gene which is highly expressed in liver, intestine, and kidney. Interestingly, eight homologous Ces2 (Ces2a to Ces2h) genes exist in mice and the individual roles of the corresponding proteins are incompletely understood. Mouse Ces2c (mCes2c) is suggested as potential ortholog of human CES2. Therefore, we aimed at its structural and biophysical characterization. Here, we present the first crystal structure of mCes2c to 2.12 A resolution. The overall structure of mCes2c resembles that of the human CES1 (hCES1). The core domain adopts an alpha/beta hydrolase-fold with S230, E347, and H459 forming a catalytic triad. Access to the active site is restricted by the cap, the flexible lid, and the regulatory domain. The conserved gate (M417) and switch (F418) residues might have a function in product release similar as suggested for hCES1. Biophysical characterization confirms that mCes2c is a monomer in solution. Thus, this study broadens our understanding of the mammalian carboxylesterase family and assists in delineating the similarities and differences of the different family members. The Crystal Structure of Mouse Ces2c, a Potential Ortholog of Human CES2, Shows Structural Similarities in Substrate Regulation and Product Release to Human CES1.,Eisner H, Riegler-Berket L, Gamez CFR, Sagmeister T, Chalhoub G, Darnhofer B, Jazleena PJ, Birner-Gruenberger R, Pavkov-Keller T, Haemmerle G, Schoiswohl G, Oberer M Int J Mol Sci. 2022 Oct 28;23(21):13101. doi: 10.3390/ijms232113101. PMID:36361897 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA