4uzu: Difference between revisions
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==Three-dimensional structure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution== | ==Three-dimensional structure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution== | ||
<StructureSection load='4uzu' size='340' side='right' caption='[[4uzu]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4uzu' size='340' side='right' caption='[[4uzu]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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='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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uzu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uzu RCSB], [http://www.ebi.ac.uk/pdbsum/4uzu PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4uzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uzu OCA], [http://pdbe.org/4uzu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4uzu RCSB], [http://www.ebi.ac.uk/pdbsum/4uzu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4uzu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4uzu" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 14:51, 11 August 2016
Three-dimensional structure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolutionThree-dimensional structure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution
Structural highlights
Publication Abstract from PubMedThe enzyme-catalysed degradation of starch is central to many industrial processes, including sugar manufacture and first-generation biofuels. Classical biotechnological platforms involve steam explosion of starch followed by the action of endo-acting glycoside hydrolases termed alpha-amylases and then exo-acting alpha-glucosidases (glucoamylases) to yield glucose, which is subsequently processed. A key enzymatic player in this pipeline is the `Termamyl' class of bacterial alpha-amylases and designed/evolved variants thereof. Here, the three-dimensional structure of one such Termamyl alpha-amylase variant based upon the parent Geobacillus stearothermophilus alpha-amylase is presented. The structure has been solved at 1.9 A resolution, revealing the classical three-domain fold stabilized by Ca(2+) and a Ca(2+)-Na(+)-Ca(2+) triad. As expected, the structure is similar to the G. stearothermophilus alpha-amylase but with main-chain deviations of up to 3 A in some regions, reflecting both the mutations and differing crystal-packing environments. Three-dimensional structure of a variant `Termamyl-like' Geobacillus stearothermophilus alpha-amylase at 1.9 A resolution.,Offen WA, Viksoe-Nielsen A, Borchert TV, Wilson KS, Davies GJ Acta Crystallogr F Struct Biol Commun. 2015 Jan 1;71(Pt 1):66-70. doi:, 10.1107/S2053230X14026508. Epub 2015 Jan 1. PMID:25615972[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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