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spinqualitylabelsall models 1ose, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

PORCINE PANCREATIC ALPHA-AMYLASE COMPLEXED WITH ACARBOSE

Overview

Two different crystal forms of pig pancreatic alpha-amylase isoenzyme II, (PPAII), free and complexed to a carbohydrate inhibitor (acarbose), have, been compared together and to previously reported structures of PPAI. A, crystal form obtained at 4 degrees C, containing nearly 72% solvent, made, it possible to obtain a new complex with acarbose, different from a, previous one obtained at 20 degrees C [Qian, M., Buisson, G., Duee, E., Haser, H. & Payan, F. (1994) Biochemistry 33, 6284-6294]. In the present, form, six contiguous subsites of the enzyme active site are occupied by, the carbohydrate ligand; the structural data indicate that the binding, site is capable of holding more than the five glucose units of the scheme, proposed through kinetic studies. A monosaccharide ring bridging two, protein molecules related by the crystal packing is located on the, surface, at a distance of 2.0 nm from the reducing end of the inhibitor, ligand; the symmetry-related glucose ring in the crystal lattice is found, 1.5 nm away from the non-reducing end of the inhibitor ligand.

About this Structure

1OSE is a Single protein structure of sequence from Sus scrofa with GLC, CL and CA as ligands. Active as Alpha-amylase, with EC number 3.2.1.1 Structure known Active Sites: AS1, AS2, AS3, AS4, AS5, CAL and CLO. Full crystallographic information is available from OCA.

Reference

Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose., Gilles C, Astier JP, Marchis-Mouren G, Cambillau C, Payan F, Eur J Biochem. 1996 Jun 1;238(2):561-9. PMID:8681972

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