1mxg

<table><tr><td colspan='2'>[[1mxg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"pyrococcus_furiosus_subsp._woesei"_kanoksilapatham_et_al._2004 "pyrococcus furiosus subsp. woesei" kanoksilapatham et al. 2004]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MXG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1MXG FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=ETE:2-{2-[2-2-(METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL'>ETE</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1mxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mxg OCA], [http://pdbe.org/1mxg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mxg RCSB], [http://www.ebi.ac.uk/pdbsum/1mxg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mxg ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:12482867</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1mxg" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Pyrococcus furiosus subsp. woesei kanoksilapatham et al. 2004]]

[[Category: Alpha-amylase]]

[[Category: Antranikian, G]]

[[Category: Linden, A]]

[[Category: Mayans, O]]

[[Category: Meyer-Klaucke, W]]

[[Category: Wilmanns, M]]

[[Category: Hyperthermostable]]