1mxd

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[[Image:1mxd.gif|left|200px]]
 
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{{Structure
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==Structure of a (Ca,Zn)-dependent alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei==
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|PDB= 1mxd |SIZE=350|CAPTION= <scene name='initialview01'>1mxd</scene>, resolution 2.0&Aring;
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<StructureSection load='1mxd' size='340' side='right'caption='[[1mxd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ACR:ACARBOSE'>ACR</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene>
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<table><tr><td colspan='2'>[[1mxd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_woesei Pyrococcus woesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MXD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MXD FirstGlance]. <br>
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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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</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&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AC1:6-METHYL-5-(4,5,6-TRIHYDROXY-3-HYDROXYMETHYL-CYCLOHEX-2-ENYLAMINO)-TETRAHYDRO-PYRAN-2,3,4-TRIOL'>AC1</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mxd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mxd OCA], [https://pdbe.org/1mxd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mxd RCSB], [https://www.ebi.ac.uk/pdbsum/1mxd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mxd ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q7LYT7_PYRWO Q7LYT7_PYRWO]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mx/1mxd_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1mxd ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Structure of a (Ca,Zn)-dependent alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei'''
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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:12482867<ref>PMID:12482867</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1mxd" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Amylase 3D structures|Amylase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1MXD 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=1MXD OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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]
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[[Category: Alpha-amylase]]
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[[Category: Pyrococcus woesei]]
[[Category: Pyrococcus woesei]]
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[[Category: Single protein]]
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[[Category: Antranikian G]]
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[[Category: Antranikian, G.]]
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[[Category: Linden A]]
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[[Category: Linden, A.]]
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[[Category: Mayans O]]
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[[Category: Mayans, O.]]
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[[Category: Meyer-Klaucke W]]
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[[Category: Meyer-Klaucke, W.]]
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[[Category: Wilmanns M]]
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[[Category: Wilmanns, M.]]
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[[Category: ACR]]
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[[Category: ACT]]
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[[Category: CA]]
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[[Category: GLC]]
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[[Category: ZN]]
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[[Category: (beta/alpha)8-barrel]]
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[[Category: alpha-amylase]]
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[[Category: family 13 glycosyl hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:49:24 2008''
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Current revision

Structure of a (Ca,Zn)-dependent alpha-amylase from the hyperthermophilic archaeon Pyrococcus woesei

PDB ID 1mxd

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