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6EMI

Crystal structure of a variant of human butyrylcholinesterase expressed in bacteria.

Summary for 6EMI
Entry DOI10.2210/pdb6emi/pdb
DescriptorCholinesterase, 1,2-ETHANEDIOL, DI(HYDROXYETHYL)ETHER, ... (7 entities in total)
Functional Keywordsalpha-beta hydrolase, prokaryotic expression, dimeric form, disulfide bond., hydrolase
Biological sourceHomo sapiens (Human)
Cellular locationSecreted : P06276
Total number of polymer chains2
Total formula weight123727.68
Authors
Brazzolotto, X.,Igert, A.,Guillon, V.,Santoni, G.,Nachon, F. (deposition date: 2017-10-02, release date: 2017-11-08, Last modification date: 2024-11-06)
Primary citationBrazzolotto, X.,Igert, A.,Guillon, V.,Santoni, G.,Nachon, F.
Bacterial Expression of Human Butyrylcholinesterase as a Tool for Nerve Agent Bioscavengers Development.
Molecules, 22:-, 2017
Cited by
PubMed Abstract: Human butyrylcholinesterase is a performant stoichiometric bioscavenger of organophosphorous nerve agents. It is either isolated from outdated plasma or functionally expressed in eukaryotic systems. Here, we report the production of active human butyrylcholinesterase in a prokaryotic system after optimization of the primary sequence through the Protein Repair One Stop Shop process, a structure- and sequence-based algorithm for soluble bacterial expression of difficult eukaryotic proteins. The mutant enzyme was purified to homogeneity. Its kinetic parameters with substrate are similar to the endogenous human butyrylcholinesterase or recombinants produced in eukaryotic systems. The isolated protein was prone to crystallize and its 2.5-Å X-ray structure revealed an active site gorge region identical to that of previously solved structures. The advantages of this alternate expression system, particularly for the generation of butyrylcholinesterase variants with nerve agent hydrolysis activity, are discussed.
PubMed: 29077024
DOI: 10.3390/molecules22111828
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.476 Å)
Structure validation

238895

数据于2025-07-16公开中

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