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== | |||
<StructureSection load='4uzu' size='340' side='right'caption='[[4uzu]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4uzu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UZU FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4uzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uzu OCA], [https://pdbe.org/4uzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4uzu RCSB], [https://www.ebi.ac.uk/pdbsum/4uzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4uzu ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AMY_GEOSE AMY_GEOSE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 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<ref>PMID:25615972</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4uzu" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Amylase 3D structures|Amylase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Geobacillus stearothermophilus]] | |||
[[Category: Large Structures]] | |||
[[Category: Anderson C]] | |||
[[Category: Borchert TV]] | |||
[[Category: Davies GJ]] | |||
[[Category: Offen WA]] | |||
[[Category: Wilson KS]] | |||
Latest revision as of 13:38, 10 January 2024
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
FunctionPublication 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. See AlsoReferences
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