2VT7

Native Torpedo californica acetylcholinesterase collected with a cumulated dose of 800000 Gy

Summary for 2VT7

• Entry DOI: 10.2210/pdb2vt7/pdb
• Related: 1ACJ 1ACL 1AMN 1AX9 1CFJ 1DX6 1E3Q 1E66 1EA5 1EEA 1EVE 1FSS 1GPK 1GPN 1GQR 1GQS 1H22 1H23 1HBJ 1JGA 1JGB 1JJB 1OCE 1ODC 1QID 1QIE 1QIF 1QIG 1QIH 1QII 1QIJ 1QIK 1QIM 1QTI 1SOM 1U65 1UT6 1VOT 1VXO 1VXR 1W4L 1W6R 1W75 1W76 1ZGB 1ZGC 2ACE 2ACK 2C4H 2C58 2C5F 2C5G 2CEK 2CKM 2CMF 2DFP 2J3D 2J3Q 2J4F 2V96 2V97 2V98 2VA9 2VJA 2VJB 2VJC 2VJD 2VQ6 2VT6 2VT7 3ACE 4ACE
• Descriptor: ACETYLCHOLINESTERASE, 2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: serine esterase, alternative splicing, native torpedo californica acetylcholinesterase, neurotransmitter degradation, lipoprotein, glycoprotein, cell junction, synapse, membrane, hydrolase, gpi-anchor
• Biological source: TORPEDO CALIFORNICA (PACIFIC ELECTRIC RAY)
• Total number of polymer chains: 2
• Total formula weight: 123630.15

Authors

Colletier, J.P.,Bourgeois, D.,Sanson, B.,Fournier, D.,Sussman, J.L.,Silman, I.,Weik, M. (deposition date: 2008-05-09, release date: 2008-07-22, Last modification date: 2023-12-13)

Primary citation

Colletier, J.P.,Bourgeois, D.,Sanson, B.,Fournier, D.,Sussman, J.L.,Silman, I.,Weik, M.
Shoot-and-Trap: Use of Specific X-Ray Damage to Study Structural Protein Dynamics by Temperature-Controlled Cryo-Crystallography.
Proc.Natl.Acad.Sci.USA, 105:11742-, 2008

PubMed Abstract: Although x-ray crystallography is the most widely used method for macromolecular structure determination, it does not provide dynamical information, and either experimental tricks or complementary experiments must be used to overcome the inherently static nature of crystallographic structures. Here we used specific x-ray damage during temperature-controlled crystallographic experiments at a third-generation synchrotron source to trigger and monitor (Shoot-and-Trap) structural changes putatively involved in an enzymatic reaction. In particular, a nonhydrolyzable substrate analogue of acetylcholinesterase, the "off-switch" at cholinergic synapses, was radiocleaved within the buried enzymatic active site. Subsequent product clearance, observed at 150 K but not at 100 K, indicated exit from the active site possibly via a "backdoor." The simple strategy described here is, in principle, applicable to any enzyme whose structure in complex with a substrate analogue is available and, therefore, could serve as a standard procedure in kinetic crystallography studies.

PubMed: 18701720
DOI: 10.1073/PNAS.0804828105

Experimental method

X-RAY DIFFRACTION (2.2 Å)