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[[Image:1wo2.gif|left|200px]]
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{{STRUCTURE_1wo2|  PDB=1wo2  |  SCENE=  }}
'''Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion'''


==Crystal structure of the pig pancreatic alpha-amylase complexed with malto-oligosaacharides under the effect of the chloride ion==
<StructureSection load='1wo2' size='340' side='right'caption='[[1wo2]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wo2]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WO2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene>, <scene name='pdbligand=PRD_900018:beta-maltose'>PRD_900018</scene>, <scene name='pdbligand=PRD_900065:beta-maltotriose'>PRD_900065</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wo2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wo2 OCA], [https://pdbe.org/1wo2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wo2 RCSB], [https://www.ebi.ac.uk/pdbsum/1wo2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wo2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMYP_PIG AMYP_PIG]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wo/1wo2_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wo2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:15736930</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1wo2" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Amylase 3D structures|Amylase 3D structures]]
[[Category: Alpha-amylase]]
== References ==
[[Category: Single protein]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Nahoum, V.]]
[[Category: Nahoum V]]
[[Category: Payan, F.]]
[[Category: Payan F]]
[[Category: Qian, M.]]
[[Category: Qian M]]
[[Category: Beta-alpha-barrel]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:55:59 2008''

Latest revision as of 16:46, 9 May 2024

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

Structural highlights

1wo2 is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.01Å
Ligands:, , , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AMYP_PIG

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Qian M, Ajandouz el H, Payan F, Nahoum V. Molecular basis of the effects of chloride ion on the acid-base catalyst in the mechanism of pancreatic alpha-amylase. Biochemistry. 2005 Mar 8;44(9):3194-201. PMID:15736930 doi:10.1021/bi048201t

1wo2, resolution 2.01Å

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