1wo2

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(New page: 200px<br /><applet load="1wo2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wo2, resolution 2.01&Aring;" /> '''Crystal structure of...)
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[[Image:1wo2.gif|left|200px]]<br /><applet load="1wo2" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1wo2.gif|left|200px]]<br /><applet load="1wo2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1wo2, resolution 2.01&Aring;" />
caption="1wo2, resolution 2.01&Aring;" />
'''Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion'''<br />
'''Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion'''<br />
==Overview==
==Overview==
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Pig pancreatic alpha-amylase (PPA), an enzyme belonging to the, alpha-amylase family, is involved in the degradation of starch. Like some, other members of this family, PPA requires chloride to reach maximum, activity levels. To further explain the mechanism of chloride activation, a crystal of wild-type PPA soaked with maltopentaose using a chloride-free, buffer was analyzed by X-ray crystallography. A conspicuous reorientation, of the acid/base catalyst Glu233 residue was found to occur. The, structural results, along with kinetic data, show that the acid/base, catalyst is maintained in the active site, in an optimum position, pointing toward the scissile bond-atom, due to the presence of chloride, ions. The present study therefore explains the mechanism of PPA activation, by chloride ions.
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Pig pancreatic alpha-amylase (PPA), an enzyme belonging to the alpha-amylase family, is involved in the degradation of starch. Like some other members of this family, PPA requires chloride to reach maximum activity levels. To further explain the mechanism of chloride activation, a crystal of wild-type PPA soaked with maltopentaose using a chloride-free buffer was analyzed by X-ray crystallography. A conspicuous reorientation of the acid/base catalyst Glu233 residue was found to occur. The structural results, along with kinetic data, show that the acid/base catalyst is maintained in the active site, in an optimum position, pointing toward the scissile bond-atom, due to the presence of chloride ions. The present study therefore explains the mechanism of PPA activation by chloride ions.
==About this Structure==
==About this Structure==
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1WO2 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 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=1WO2 OCA].
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1WO2 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=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=1WO2 OCA].
==Reference==
==Reference==
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[[Category: beta-alpha-barrels]]
[[Category: beta-alpha-barrels]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:33:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:46:26 2008''

Revision as of 13:46, 21 February 2008

Image:1wo2.gif

1wo2, resolution 2.01Å

Drag the structure with the mouse to rotate

Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion

Overview

Pig pancreatic alpha-amylase (PPA), an enzyme belonging to the alpha-amylase family, is involved in the degradation of starch. Like some other members of this family, PPA requires chloride to reach maximum activity levels. To further explain the mechanism of chloride activation, a crystal of wild-type PPA soaked with maltopentaose using a chloride-free buffer was analyzed by X-ray crystallography. A conspicuous reorientation of the acid/base catalyst Glu233 residue was found to occur. The structural results, along with kinetic data, show that the acid/base catalyst is maintained in the active site, in an optimum position, pointing toward the scissile bond-atom, due to the presence of chloride ions. The present study therefore explains the mechanism of PPA activation by chloride ions.

About this Structure

1WO2 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

Molecular basis of the effects of chloride ion on the acid-base catalyst in the mechanism of pancreatic alpha-amylase., Qian M, Ajandouz el H, Payan F, Nahoum V, Biochemistry. 2005 Mar 8;44(9):3194-201. PMID:15736930

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