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1hx0

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(New page: 200px<br /><applet load="1hx0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hx0, resolution 1.38&Aring;" /> '''STRUCTURE OF PIG PAN...)
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[[Image:1hx0.gif|left|200px]]<br /><applet load="1hx0" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1hx0, resolution 1.38&Aring;" />
caption="1hx0, resolution 1.38&Aring;" />
'''STRUCTURE OF PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE "TRUNCATE" ACARBOSE MOLECULE (PSEUDOTRISACCHARIDE)'''<br />
'''STRUCTURE OF PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE "TRUNCATE" ACARBOSE MOLECULE (PSEUDOTRISACCHARIDE)'''<br />
==Overview==
==Overview==
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Mammalian alpha-amylases catalyze the hydrolysis of alpha-linked glucose, polymers according to a complex processive mechanism. We have determined, the X-ray structures of porcine pancreatic alpha-amylase complexes with, the smallest molecule of the trestatin family (acarviosine-glucose) which, inhibits porcine pancreatic alpha-amylase and yet is not hydrolyzed by the, enzyme. A structure analysis at 1.38 A resolution of this complex allowed, for a clear identification of a genuine single hexasaccharide species, composed of two alpha-1,4-linked original molecules bound to the active, site of the enzyme. The structural results supported by mass spectrometry, experiments provide evidence for an enzymatically catalyzed condensation, reaction in the crystal.
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Mammalian alpha-amylases catalyze the hydrolysis of alpha-linked glucose polymers according to a complex processive mechanism. We have determined the X-ray structures of porcine pancreatic alpha-amylase complexes with the smallest molecule of the trestatin family (acarviosine-glucose) which inhibits porcine pancreatic alpha-amylase and yet is not hydrolyzed by the enzyme. A structure analysis at 1.38 A resolution of this complex allowed for a clear identification of a genuine single hexasaccharide species composed of two alpha-1,4-linked original molecules bound to the active site of the enzyme. The structural results supported by mass spectrometry experiments provide evidence for an enzymatically catalyzed condensation reaction in the crystal.
==About this Structure==
==About this Structure==
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1HX0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with MAL, CL, CA and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HX0 OCA].
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1HX0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=MAL:'>MAL</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HX0 OCA].
==Reference==
==Reference==
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[[Category: pancreas]]
[[Category: pancreas]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:52:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:05:38 2008''

Revision as of 11:05, 21 February 2008

Image:1hx0.gif

1hx0, resolution 1.38Å

Drag the structure with the mouse to rotate

STRUCTURE OF PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE "TRUNCATE" ACARBOSE MOLECULE (PSEUDOTRISACCHARIDE)

Overview

Mammalian alpha-amylases catalyze the hydrolysis of alpha-linked glucose polymers according to a complex processive mechanism. We have determined the X-ray structures of porcine pancreatic alpha-amylase complexes with the smallest molecule of the trestatin family (acarviosine-glucose) which inhibits porcine pancreatic alpha-amylase and yet is not hydrolyzed by the enzyme. A structure analysis at 1.38 A resolution of this complex allowed for a clear identification of a genuine single hexasaccharide species composed of two alpha-1,4-linked original molecules bound to the active site of the enzyme. The structural results supported by mass spectrometry experiments provide evidence for an enzymatically catalyzed condensation reaction in the crystal.

About this Structure

1HX0 is a Single protein structure of sequence from Sus scrofa with , , and as ligands. Active as Alpha-amylase, with EC number 3.2.1.1 Full crystallographic information is available from OCA.

Reference

Enzyme-catalyzed condensation reaction in a mammalian alpha-amylase. High-resolution structural analysis of an enzyme-inhibitor complex., Qian M, Nahoum V, Bonicel J, Bischoff H, Henrissat B, Payan F, Biochemistry. 2001 Jun 26;40(25):7700-9. PMID:11412124

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