4e2o: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4e2o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_thermoleovorans_CCB_US3_UF5 Geobacillus thermoleovorans CCB_US3_UF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E2O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E2O FirstGlance]. <br> | <table><tr><td colspan='2'>[[4e2o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_thermoleovorans_CCB_US3_UF5 Geobacillus thermoleovorans CCB_US3_UF5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E2O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E2O FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACI:6-AMINO-4-HYDROXYMETHYL-CYCLOHEX-4-ENE-1,2,3-TRIOL'>ACI</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=G6D:6-DEOXY-ALPHA-D-GLUCOSE'>G6D</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.103Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACI:6-AMINO-4-HYDROXYMETHYL-CYCLOHEX-4-ENE-1,2,3-TRIOL'>ACI</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=G6D:6-DEOXY-ALPHA-D-GLUCOSE'>G6D</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</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=4e2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e2o OCA], [https://pdbe.org/4e2o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e2o RCSB], [https://www.ebi.ac.uk/pdbsum/4e2o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e2o ProSAT]</span></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=4e2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e2o OCA], [https://pdbe.org/4e2o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e2o RCSB], [https://www.ebi.ac.uk/pdbsum/4e2o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e2o ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/G8N704_GEOTH G8N704_GEOTH] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Latest revision as of 16:45, 8 November 2023
Crystal structure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarboseCrystal structure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose
Structural highlights
FunctionPublication Abstract from PubMedA truncated form of an alpha-amylase, GTA, from thermophilic Geobacillus thermoleovorans CCB_US3_UF5 was biochemically and structurally characterized. The recombinant GTA, which lacked both the N- and C-terminal transmembrane regions, functioned optimally at 70 degrees C and pH 6.0. While enzyme activity was not enhanced by the addition of CaCl2, GTA's thermostability was significantly improved in the presence of CaCl2. The structure, in complex with an acarbose-derived pseudo-hexasaccharide, consists of the typical three domains and binds one Ca(2+) ion. This Ca(2+) ion was strongly bound and not chelated by EDTA. A predicted second Ca(2+)-binding site, however, was disordered. With limited subsites, two novel substrate-binding residues, Y147 and Y182, may help increase substrate affinity. No distinct starch-binding domain is present, although two regions rich in aromatic residues have been observed. GTA, with a smaller domain B and several shorter loops compared to other alpha-amylases, has one of the most compact alpha-amylase folds that may contribute greatly to its tight Ca(2+) binding and thermostability. Crystal structure of a compact alpha-amylase from Geobacillus thermoleovorans.,Mok SC, Teh AH, Saito JA, Najimudin N, Alam M Enzyme Microb Technol. 2013 Jun 10;53(1):46-54. doi:, 10.1016/j.enzmictec.2013.03.009. Epub 2013 Mar 28. PMID:23683704[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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