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6xsv
From Proteopedia
(Difference between revisions)
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<StructureSection load='6xsv' size='340' side='right'caption='[[6xsv]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='6xsv' size='340' side='right'caption='[[6xsv]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XSV 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]] 1.65Å</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]] 1.65Å</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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene></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=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</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=6xsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xsv OCA], [https://pdbe.org/6xsv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xsv RCSB], [https://www.ebi.ac.uk/pdbsum/6xsv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xsv 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=6xsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xsv OCA], [https://pdbe.org/6xsv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xsv RCSB], [https://www.ebi.ac.uk/pdbsum/6xsv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xsv ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Function == | ||
| - | [https://www.uniprot.org/uniprot/AMYA1_ASPOR AMYA1_ASPOR] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The structures of Aspergillus oryzae alpha-amylase were determined in a tetragonal crystal, having one molecule as asymmetric unit, and a monoclinic crystal with two molecules as asymmetric unit. Both crystal forms were obtained from trace contaminants of an old commercial lipase preparation. Structures were determined and refined to 1.65 A and 1.43 A resolution respectively. The latter crystal has a non-crystallographic (NCS) twofold axis within the asymmetric unit. Glycosylation at Asn197 is evident, and in the tetragonal crystal can be seen to include three, partially disordered sugar residues following the initial N-acetyl glucosamine (NAG). Superposition of the tetragonal crystal model on the alpha-amylases from Bacillus subtilis (PDB:1BAG), pig pancreas (PDB:3L2L), and barley (PDB:1AMY), show a high degree of coincidence, particularly for the (beta/alpha)8-barrel domains, and especially within the active site. Using this structural agreement between amylases, we extrapolated the binding model of a six residue, limit dextrin found in pig pancreas alpha-amylase to the A. oryzae enzyme model, which predicts substrate interacting amino acid residues. | ||
| - | |||
| - | Structures of two novel crystal forms of Aspergillus oryzae alpha amylase (taka-amylase).,Gee CL, Holton JM, McPherson A J Biosci Bioeng. 2021 Apr 2. pii: S1389-1723(21)00053-0. doi:, 10.1016/j.jbiosc.2021.02.008. PMID:33814275<ref>PMID:33814275</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 6xsv" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Amylase 3D structures|Amylase 3D structures]] | *[[Amylase 3D structures|Amylase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Aspergillus oryzae]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: McPherson A]] | [[Category: McPherson A]] | ||
Current revision
X-ray structure of a tetragonal crystal form of alpha amylase from Aspergillus oryzae (Tala-Amylase) at 1.65 A resolution
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