Essential arginine residue in acetylcholinesterase from Torpedo californica
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چکیده
منابع مشابه
Active-site gorge and buried water molecules in crystal structures of acetylcholinesterase from Torpedo californica.
Buried water molecules and the water molecules in the active-site gorge are analyzed for five crystal structures of acetylcholinesterase from Torpedo californica in the resolution range 2.2-2.5 A (native enzyme, and four inhibitor complexes). A total of 45 buried hydration sites are identified, which are populated with between 36 and 41 water molecules. About half of the buried water is located...
متن کاملAtomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein.
The three-dimensional structure of acetylcholinesterase from Torpedo californica electric organ has been determined by x-ray analysis to 2.8 angstrom resolution. The form crystallized is the glycolipid-anchored homodimer that was purified subsequent to solubilization with a bacterial phosphatidylinositol-specific phospholipase C. The enzyme monomer is an alpha/beta protein that contains 537 ami...
متن کاملTorpedo californica electroplax
Polyclonal rabbit antibodies were raised against 4-acetamido-4'-isothiocyanostilbene-2,2'-disulphonic acid (SITS), an inhibitor of a variety of anion transport proteins. These antibodies specifically recognize SITSreacted erythrocyte band 3 in immunoprecipitations and Western blots. In Western blots of SITS-reacted membrane proteins derived from vesicles of the electric organ of Torpedo califor...
متن کاملAn Essential Arginine Residue in Porcine Phospholipase
Reaction of phenylglyoxal, a reagent specific for arginine residues, with porcine phospholipase Az results in complete elimination of catalytic activity. The modification reaction is markedly dependent on pH. Other dicarbonyl compounds such as 2,3-butanedione and 1,2cyclohexanedione also react with the enzyme to cause loss of activity but at significantly slower rates. At pH 7.0, the inactivati...
متن کاملStructure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesterase.
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 dif...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1980
ISSN: 0014-5793
DOI: 10.1016/0014-5793(80)80272-9