View source for 4uzu


==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]] 1.90&Aring;' 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]] 1.9&#8491;</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&reg;/PubMed&reg;, 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]]