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Publication Abstract from PubMed

GDSL esterase J15 (EstJ15) is a member of Family II of lipolytic enzyme. The enzyme was further classified in subgroup SGNH hydrolase due to the presence of highly conserve motif, Ser-Gly-Asn-His in four conserved blocks I, II, III, and V, respectively. X-ray quality crystal of EstJ15 was obtained from optimized formulation containing 0.10M ammonium sulphate, 0.15M sodium cacodylate trihydrate pH6.5, and 20% PEG 8000. The crystal structure of EstJ15 was solved at 1.38A with one molecule per asymmetric unit. The structure exhibits alpha/beta hydrolase fold and shared low amino acid sequence identity of 23% with the passenger domain of the autotransporter EstA of Pseudomonas aeruginosa. The active site is located at the centre of the structure, formed a narrow tunnel that hinder long substrates to be catalysed which was proven by the protein-ligand docking analysis. This study facilitates the understanding of high substrate specificity of EstJ15 and provide insights on its catalytic mechanism.

Crystallization and structure elucidation of GDSL esterase of Photobacterium sp. J15.,Mazlan SNHS, Ali MSM, Rahman RNZRA, Sabri S, Jonet MA, Leow TC Int J Biol Macromol. 2018 Nov;119:1188-1194. doi: 10.1016/j.ijbiomac.2018.08.022., Epub 2018 Aug 10. PMID:30102982^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.