A novel acetate-bound complex of human carbonic anhydrase II.
The enzyme human carbonic anhydrase II (hCAII) crystallized in an acetate-bound complex belonging to space group P2(1)2(1)2(1), with unit-cell parameters a = 42.3, b = 71.8, c = 74.0 A. The structure was solved by the molecular-replacement method and refined to an R value of 0.18 and an R(free) of 0.21. The acetate molecule replaced the zinc-bound water molecule in the structure, differing from previous reports regarding the site of acetate binding. This mode of binding disrupts the hydrogen-bonded solvent network required for activity of the enzyme. This mode of inhibitor binding is a novel one that has not been observed previously.
Mazumdar
Pooja Anjali
PA
Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur 721302, India.
Kumaran
Desigan
D
Swaminathan
Subramanyam
S
Das
Amit Kumar
AK
D000085:Acetates / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D024402:Carbonic Anhydrase II / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D018360:Crystallography, X-Ray; D006801:Humans; D006860:Hydrogen Bonding; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D012997:Solvents
D000085:Acetates; D012997:Solvents; D024402:Carbonic Anhydrase II