1ose

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{{STRUCTURE_1ose| PDB=1ose | SCENE= }}
{{STRUCTURE_1ose| PDB=1ose | SCENE= }}
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'''PORCINE PANCREATIC ALPHA-AMYLASE COMPLEXED WITH ACARBOSE'''
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===PORCINE PANCREATIC ALPHA-AMYLASE COMPLEXED WITH ACARBOSE===
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==Overview==
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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. &amp; 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.
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{{ABSTRACT_PUBMED_8681972}}
==About this Structure==
==About this Structure==
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[[Category: Alpha-amylase]]
[[Category: Alpha-amylase]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:01:51 2008''

Revision as of 14:01, 27 July 2008

Template:STRUCTURE 1ose

PORCINE PANCREATIC ALPHA-AMYLASE COMPLEXED WITH ACARBOSE

Template:ABSTRACT PUBMED 8681972

About this Structure

1OSE is a Single protein structure of sequence from Sus scrofa. 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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