1OSE

Porcine pancreatic alpha-amylase complexed with acarbose

Summary for 1OSE

• Entry DOI: 10.2210/pdb1ose/pdb
• Descriptor: PORCINE ALPHA-AMYLASE, 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose, beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: alpha-amylase, acarbose, hydrolase (o-glycosyl), hydrolase
• Biological source: Sus scrofa (pig)
• Total number of polymer chains: 1
• Total formula weight: 56620.31

Authors

Gilles, C.,Payan, F. (deposition date: 1996-03-20, release date: 1997-04-01, Last modification date: 2024-10-09)

Primary citation

Gilles, C.,Astier, J.P.,Marchis-Mouren, G.,Cambillau, C.,Payan, F.
Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose.
Eur.J.Biochem., 238:561-569, 1996

PubMed Abstract: 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., Duée, 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.

PubMed: 8681972
DOI: 10.1111/j.1432-1033.1996.0561z.x

Experimental method

X-RAY DIFFRACTION (2.3 Å)