1wo2: Difference between revisions
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[[Image:1wo2.gif|left|200px]] | [[Image:1wo2.gif|left|200px]] | ||
'''Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion''' | {{Structure | ||
|PDB= 1wo2 |SIZE=350|CAPTION= <scene name='initialview01'>1wo2</scene>, resolution 2.01Å | |||
|SITE= | |||
|LIGAND= <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> | |||
|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] | |||
|GENE= | |||
}} | |||
'''Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1WO2 is a [ | 1WO2 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=1WO2 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15736930 15736930] | ||
[[Category: Alpha-amylase]] | [[Category: Alpha-amylase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: CL]] | [[Category: CL]] | ||
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: beta-alpha- | [[Category: beta-alpha-barrel]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:59:27 2008'' | ||
Revision as of 15:59, 20 March 2008
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| , resolution 2.01Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Activity: | Alpha-amylase, with EC number 3.2.1.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion
OverviewOverview
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 StructureAbout this Structure
1WO2 is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
ReferenceReference
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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