1E3Q

TORPEDO CALIFORNICA ACETYLCHOLINESTERASE COMPLEXED WITH BW284C51

Summary for 1E3Q

• Entry DOI: 10.2210/pdb1e3q/pdb
• Related: 1ACJ 1ACL 1AMN 1AX9 1CFJ 1EEA 1EVE 1FSS 1OCE 1QID 1QIE 1QIF 1QIG 1QIH 1QII 1QIJ 1QIK 1QIM 1QTI 1SOM 1VOT 1VXO 1VXR 2ACE 2ACK 2DFP 2DX6 3ACE 4ACE
• Descriptor: ACETYLCHOLINESTERASE, 4-(5-{4-[DIMETHYL(PROP-2-ENYL)AMMONIO]PHENYL}-3-OXOPENTYL)-N,N-DIMETHYL-N-PROP-2-ENYLBENZENAMINIUM, SULFATE ION, ... (5 entities in total)
• Functional Keywords: serine hydrolase, hydrolase, inhibitor
• Biological source: TORPEDO CALIFORNICA (PACIFIC ELECTRIC RAY)
• Cellular location: Isoform H: Cell membrane; Lipid-anchor, GPI- anchor. Isoform T: Cell membrane; Peripheral membrane protein: P04058
• Total number of polymer chains: 1
• Total formula weight: 62491.38

Authors

Felder, C.E.,Harel, M.,Silman, I.,Sussman, J.L. (deposition date: 2000-06-21, release date: 2000-07-03, Last modification date: 2024-10-16)

Primary citation

Felder, C.E.,Harel, M.,Silman, I.,Sussman, J.L.
Structure of a Complex of the Potent and Specific Inhibitor Bw284C51 with Torpedo Californica Acetylcholinesterase
Acta Crystallogr.,Sect.D, 58:1765-, 2002

PubMed Abstract: The X-ray crystal structure of Torpedo californica acetylcholinesterase (TcAChE) complexed with BW284C51 [CO[-CH(2)CH(2)-pC(6)H(4)-N(CH(3))(2)(CH(2)-CH=CH(2))](2)] is described and compared with the complexes of two other active-site gorge-spanning inhibitors, decamethonium and E2020. The inhibitor was soaked into TcAChE crystals in the trigonal space group P3(1)21, yielding a complex which diffracted to 2.85 A resolution. The structure was refined to an R factor of 19.0% and an R(free) of 23.4%; the final model contains the protein, inhibitor, 132 water molecules and three carbohydrate moieties. BW284C51 binds similarly to decamethonium and E2020, with its two phenyl and quaternary amino end-groups complexed to Trp84 in the catalytic site and to Trp279 in the peripheral binding site, and its central carbonyl group hydrogen bonded very weakly to Tyr121. Possible reasons for decamethonium's weaker binding are considered. The relative strength of binding of bisquaternary inhibitors to acetylcholinesterase and the effect of several mutations of the enzyme are discussed in the context of the respective X-ray structures of their complexes with the enzyme.

PubMed: 12351819
DOI: 10.1107/S0907444902011642

Experimental method

X-RAY DIFFRACTION (2.85 Å)