6m4m: Difference between revisions
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The | ==X-ray crystal structure of the E249Q mutan of alpha-amylase I and maltohexaose complex from Eisenia fetida== | ||
<StructureSection load='6m4m' size='340' side='right'caption='[[6m4m]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6M4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6M4M 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]] 1.7Å</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=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PRD_900010:alpha-maltotetraose'>PRD_900010</scene>, <scene name='pdbligand=PRD_900035:alpha-maltohexaose'>PRD_900035</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6m4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6m4m OCA], [https://pdbe.org/6m4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6m4m RCSB], [https://www.ebi.ac.uk/pdbsum/6m4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6m4m ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The earthworm Eisenia fetida possesses several cold-active enzymes, including alpha-amylase, beta-glucanase and beta-mannanase. E. fetida possesses two isoforms of alpha-amylase (Ef-Amy I and II) to digest raw starch. Ef-Amy I retains its catalytic activity at temperatures below 10 degrees C. To identify the molecular properties of Ef-Amy I, X-ray crystal structures were determined of the wild type and of the inactive E249Q mutant. Ef-Amy I has structural similarities to mammalian alpha-amylases, including the porcine pancreatic and human pancreatic alpha-amylases. Structural comparisons of the overall structures as well as of the Ca(2+)-binding sites of Ef-Amy I and the mammalian alpha-amylases indicate that Ef-Amy I has increased structural flexibility and more solvent-exposed acidic residues. These structural features of Ef-Amy I may contribute to its observed catalytic activity at low temperatures, as many cold-adapted enzymes have similar structural properties. The structure of the substrate complex of the inactive mutant of Ef-Amy I shows that a maltohexaose molecule is bound in the active site and a maltotetraose molecule is bound in the cleft between the N- and C-terminal domains. The recognition of substrate molecules by Ef-Amy I exhibits some differences from that observed in structures of human pancreatic alpha-amylase. This result provides insights into the structural modulation of the recognition of substrates and inhibitors. | |||
X-ray crystallographic structural studies of alpha-amylase I from Eisenia fetida.,Hirano Y, Tsukamoto K, Ariki S, Naka Y, Ueda M, Tamada T Acta Crystallogr D Struct Biol. 2020 Sep 1;76(Pt 9):834-844. doi:, 10.1107/S2059798320010165. Epub 2020 Aug 25. PMID:32876059<ref>PMID:32876059</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Ariki | <div class="pdbe-citations 6m4m" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Amylase 3D structures|Amylase 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Ariki S]] | |||
[[Category: Hirano Y]] | |||
[[Category: Naka Y]] | |||
[[Category: Tamada T]] | |||
[[Category: Tsukamoto K]] | |||
[[Category: Ueda M]] | |||
Latest revision as of 10:11, 23 October 2024
X-ray crystal structure of the E249Q mutan of alpha-amylase I and maltohexaose complex from Eisenia fetida
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