1mxg

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[[Image:1mxg.gif|left|200px]]<br /><applet load="1mxg" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1mxg.gif|left|200px]]
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caption="1mxg, resolution 1.6&Aring;" />
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'''Crystal Strucutre of a (Ca,Zn)-dependent alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei in complex with acarbose'''<br />
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{{Structure
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|PDB= 1mxg |SIZE=350|CAPTION= <scene name='initialview01'>1mxg</scene>, resolution 1.6&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ACR:ACARBOSE'>ACR</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ETE:2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>ETE</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> and <scene name='pdbligand=EOH:ETHANOL'>EOH</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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'''Crystal Strucutre of a (Ca,Zn)-dependent alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei in complex with acarbose'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1MXG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_woesei Pyrococcus woesei] with <scene name='pdbligand=ACR:'>ACR</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ETE:'>ETE</scene>, <scene name='pdbligand=TRS:'>TRS</scene> and <scene name='pdbligand=EOH:'>EOH</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=1MXG OCA].
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1MXG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_woesei Pyrococcus woesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MXG OCA].
==Reference==
==Reference==
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Differential regulation of a hyperthermophilic alpha-amylase with a novel (Ca,Zn) two-metal center by zinc., Linden A, Mayans O, Meyer-Klaucke W, Antranikian G, Wilmanns M, J Biol Chem. 2003 Mar 14;278(11):9875-84. Epub 2002 Dec 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12482867 12482867]
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Differential regulation of a hyperthermophilic alpha-amylase with a novel (Ca,Zn) two-metal center by zinc., Linden A, Mayans O, Meyer-Klaucke W, Antranikian G, Wilmanns M, J Biol Chem. 2003 Mar 14;278(11):9875-84. Epub 2002 Dec 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12482867 12482867]
[[Category: Alpha-amylase]]
[[Category: Alpha-amylase]]
[[Category: Pyrococcus woesei]]
[[Category: Pyrococcus woesei]]
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[[Category: hyperthermostable]]
[[Category: hyperthermostable]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:00:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:49:26 2008''

Revision as of 10:49, 20 March 2008

Image:1mxg.gif


PDB ID 1mxg

Drag the structure with the mouse to rotate
, resolution 1.6Å
Ligands: , , , , , and
Activity: Alpha-amylase, with EC number 3.2.1.1
Coordinates: save as pdb, mmCIF, xml



Crystal Strucutre of a (Ca,Zn)-dependent alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei in complex with acarbose


Overview

The crystal structure of the alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei was solved in the presence of three inhibitors: acarbose, Tris, and zinc. In the absence of exogenous metals, this alpha-amylase bound 1 and 4 molar eq of zinc and calcium, respectively. The structure reveals a novel, activating, two-metal (Ca,Zn)-binding site and a second inhibitory zinc-binding site that is found in the -1 sugar-binding pocket within the active site. The data resolve the apparent paradox between the zinc requirement for catalytic activity and its strong inhibitory effect when added in molar excess. They provide a rationale as to why this alpha-amylase, in contrast to commercially available alpha-amylases, does not require the addition of metal ions for full catalytic activity, suggesting it as an ideal target to maximize the efficiency of industrial processes like liquefaction of starch.

About this Structure

1MXG is a Single protein structure of sequence from Pyrococcus woesei. Full crystallographic information is available from OCA.

Reference

Differential regulation of a hyperthermophilic alpha-amylase with a novel (Ca,Zn) two-metal center by zinc., Linden A, Mayans O, Meyer-Klaucke W, Antranikian G, Wilmanns M, J Biol Chem. 2003 Mar 14;278(11):9875-84. Epub 2002 Dec 12. PMID:12482867

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