6xsj
From Proteopedia
(Difference between revisions)
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==X-ray structure of a monoclinic form of alpha amylase from Aspergillus at 1.4 A resolution== | ==X-ray structure of a monoclinic form of alpha amylase from Aspergillus at 1.4 A resolution== | ||
| - | <StructureSection load='6xsj' size='340' side='right'caption='[[6xsj]]' scene=''> | + | <StructureSection load='6xsj' size='340' side='right'caption='[[6xsj]], [[Resolution|resolution]] 1.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XSJ OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6xsj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspoz Aspoz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XSJ FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rhaG, amy3, OAory_01056410 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5062 ASPOZ])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=6xsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xsj OCA], [https://pdbe.org/6xsj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xsj RCSB], [https://www.ebi.ac.uk/pdbsum/6xsj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xsj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <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 6xsj" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Amylase 3D structures|Amylase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Alpha-amylase]] | ||
| + | [[Category: Aspoz]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: McPherson A]] | + | [[Category: McPherson, A]] |
| + | [[Category: Catalytic site]] | ||
| + | [[Category: Homology]] | ||
| + | [[Category: Novo enzyme]] | ||
| + | [[Category: Substrate complex]] | ||
| + | [[Category: Sugar binding protein]] | ||
Revision as of 08:29, 21 April 2021
X-ray structure of a monoclinic form of alpha amylase from Aspergillus at 1.4 A resolution
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