2aaa

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(New page: 200px<br /><applet load="2aaa" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aaa, resolution 2.1&Aring;" /> '''CALCIUM BINDING IN AL...)
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[[Image:2aaa.jpg|left|200px]]<br /><applet load="2aaa" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2aaa, resolution 2.1&Aring;" />
 
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'''CALCIUM BINDING IN ALPHA-AMYLASES: AN X-RAY DIFFRACTION STUDY AT 2.1 ANGSTROMS RESOLUTION OF TWO ENZYMES FROM ASPERGILLUS'''<br />
 
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==Overview==
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==CALCIUM BINDING IN ALPHA-AMYLASES: AN X-RAY DIFFRACTION STUDY AT 2.1 ANGSTROMS RESOLUTION OF TWO ENZYMES FROM ASPERGILLUS==
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X-ray diffraction analysis (at 2.1-A resolution) of an acid alpha-amylase, from Aspergillus niger allowed a detailed description of the, stereochemistry of the calcium-binding sites. The primary site (which is, essential in maintaining proper folding around the active site) contains a, tightly bound Ca2+ with an unusually high number of eight ligands (O delta, 1 and O delta 2 of Asp175, O delta of Asn121, main-chain carbonyl oxygens, of Glu162 and Glu210, and three water molecules). A secondary binding site, was identified at the bottom of the substrate binding cleft; it involves, the residues presumed to play a catalytic role (Asp206 and Glu230). This, explains the inhibitory effect of calcium observed at higher, concentrations. Neutral Aspergillus oryzae (TAKA) alpha-amylase was also, refined in a new crystal at 2.1-A resolution. The structure of this, homologous (over 80%) enzyme and additional kinetic studies support all, the structural conclusions regarding both calcium-binding sites.
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<StructureSection load='2aaa' size='340' side='right'caption='[[2aaa]], [[Resolution|resolution]] 2.12&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2aaa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AAA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AAA FirstGlance]. <br>
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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]] 2.12&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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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=2aaa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aaa OCA], [https://pdbe.org/2aaa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aaa RCSB], [https://www.ebi.ac.uk/pdbsum/2aaa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aaa ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMYA_ASPNG AMYA_ASPNG]
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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/aa/2aaa_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=2aaa 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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X-ray diffraction analysis (at 2.1-A resolution) of an acid alpha-amylase from Aspergillus niger allowed a detailed description of the stereochemistry of the calcium-binding sites. The primary site (which is essential in maintaining proper folding around the active site) contains a tightly bound Ca2+ with an unusually high number of eight ligands (O delta 1 and O delta 2 of Asp175, O delta of Asn121, main-chain carbonyl oxygens of Glu162 and Glu210, and three water molecules). A secondary binding site was identified at the bottom of the substrate binding cleft; it involves the residues presumed to play a catalytic role (Asp206 and Glu230). This explains the inhibitory effect of calcium observed at higher concentrations. Neutral Aspergillus oryzae (TAKA) alpha-amylase was also refined in a new crystal at 2.1-A resolution. The structure of this homologous (over 80%) enzyme and additional kinetic studies support all the structural conclusions regarding both calcium-binding sites.
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==About this Structure==
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Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus.,Boel E, Brady L, Brzozowski AM, Derewenda Z, Dodson GG, Jensen VJ, Petersen SB, Swift H, Thim L, Woldike HF Biochemistry. 1990 Jul 3;29(26):6244-9. PMID:2207069<ref>PMID:2207069</ref>
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2AAA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_niger Aspergillus niger] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AAA OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Calcium binding in alpha-amylases: an X-ray diffraction study at 2.1-A resolution of two enzymes from Aspergillus., Boel E, Brady L, Brzozowski AM, Derewenda Z, Dodson GG, Jensen VJ, Petersen SB, Swift H, Thim L, Woldike HF, Biochemistry. 1990 Jul 3;29(26):6244-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2207069 2207069]
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</div>
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[[Category: Alpha-amylase]]
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<div class="pdbe-citations 2aaa" style="background-color:#fffaf0;"></div>
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[[Category: Aspergillus niger]]
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[[Category: Single protein]]
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[[Category: Brady, L.]]
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[[Category: Brzozowski, A.M.]]
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[[Category: Derewenda, Z.]]
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[[Category: Dodson, E.J.]]
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[[Category: Dodson, G.G.]]
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[[Category: CA]]
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[[Category: glycosidase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:00:46 2007''
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==See Also==
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*[[Amylase 3D structures|Amylase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Aspergillus niger]]
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[[Category: Large Structures]]
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[[Category: Brady L]]
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[[Category: Brzozowski AM]]
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[[Category: Derewenda Z]]
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[[Category: Dodson EJ]]
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[[Category: Dodson GG]]

Current revision

CALCIUM BINDING IN ALPHA-AMYLASES: AN X-RAY DIFFRACTION STUDY AT 2.1 ANGSTROMS RESOLUTION OF TWO ENZYMES FROM ASPERGILLUS

PDB ID 2aaa

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