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1hx0

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[[Image:1hx0.gif|left|200px]]<br /><applet load="1hx0" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1hx0.gif|left|200px]]
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caption="1hx0, resolution 1.38&Aring;" />
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'''STRUCTURE OF PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE "TRUNCATE" ACARBOSE MOLECULE (PSEUDOTRISACCHARIDE)'''<br />
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{{Structure
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|PDB= 1hx0 |SIZE=350|CAPTION= <scene name='initialview01'>1hx0</scene>, resolution 1.38&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''STRUCTURE OF PIG PANCREATIC ALPHA-AMYLASE COMPLEXED WITH THE "TRUNCATE" ACARBOSE MOLECULE (PSEUDOTRISACCHARIDE)'''
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==Overview==
==Overview==
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==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 <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].
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1HX0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HX0 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11412124 11412124]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11412124 11412124]
[[Category: Alpha-amylase]]
[[Category: Alpha-amylase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: carbohydrate]]
[[Category: carbohydrate]]
[[Category: inhibitor]]
[[Category: inhibitor]]
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[[Category: pancreas]]
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[[Category: pancrea]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:05:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:42:37 2008''

Revision as of 09:42, 20 March 2008


PDB ID 1hx0

Drag the structure with the mouse to rotate
, resolution 1.38Å
Ligands: , , and
Activity: Alpha-amylase, with EC number 3.2.1.1
Coordinates: save as pdb, mmCIF, xml



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. 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

Page seeded by OCA on Thu Mar 20 11:42:37 2008

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