1xlu

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X-Ray Structure Of Di-Isopropyl-Phosphoro-Fluoridate (Dfp) Inhibited Butyrylcholinesterase after Aging

File:1xlu.gif


1xlu, resolution 2.198Å

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OverviewOverview

Organophosphorus poisons (OP) bind covalently to the active-site serine of, cholinesterases. The inhibited enzyme can usually be reactivated with, powerful nucleophiles such as oximes. However, the covalently bound OP can, undergo a suicide reaction (termed aging) yielding nonreactivatable, enzyme. In human butyrylcholinesterase (hBChE), aging involves the, residues His438 and Glu197 that are proximal to the active-site serine, (Ser198). The mechanism of aging is known in detail for the nerve gases, soman, sarin, and tabun as well as the pesticide metabolite isomalathion., Aging of soman- and sarin-inhibited acetylcholinesterase occurs by C-O, bond cleavage, whereas that of tabun- and isomalathion-inhibited, acetylcholinesterase occurs by P-N and P-S bond cleavage, respectively. In, this work, the crystal structures of hBChE inhibited by the ophthalmic, reagents echothiophate (nonaged and aged) and diisopropylfluorophosphate, (aged) were solved and refined to 2.1, 2.25, and 2.2 A resolution, respectively. No appreciable shift in the position of the catalytic triad, histidine was observed between the aged and nonaged conjugates of hBChE., This absence of shift contrasts with the aged and nonaged crystal, structures of Torpedo californica acetylcholinesterase inhibited by the, nerve agent VX. The nonaged hBChE structure shows one water molecule, interacting with Glu197 and the catalytic triad histidine (His438)., Interestingly, this water molecule is ideally positioned to promote aging, by two mechanisms: breaking either a C-O bond or a P-O bond. Pesticides, and certain stereoisomers of nerve agents are expected to undergo aging by, breaking the P-O bond.

DiseaseDisease

Known diseases associated with this structure: Apnea, postanesthetic OMIM:[177400]

About this StructureAbout this Structure

1XLU is a Single protein structure of sequence from Homo sapiens with NAG, SO4, CL, MIP, S and GOL as ligands. Active as Cholinesterase, with EC number 3.1.1.8 Full crystallographic information is available from OCA.

ReferenceReference

Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging., Nachon F, Asojo OA, Borgstahl GE, Masson P, Lockridge O, Biochemistry. 2005 Feb 1;44(4):1154-62. PMID:15667209

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