3wn6: Difference between revisions
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The | ==Crystal structure of alpha-amylase AmyI-1 from Oryza sativa== | ||
<StructureSection load='3wn6' size='340' side='right'caption='[[3wn6]], [[Resolution|resolution]] 2.16Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3wn6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa_Japonica_Group Oryza sativa Japonica Group]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WN6 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]] 2.16Å</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=TAR:D(-)-TARTARIC+ACID'>TAR</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=3wn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wn6 OCA], [https://pdbe.org/3wn6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wn6 RCSB], [https://www.ebi.ac.uk/pdbsum/3wn6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wn6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AMY1_ORYSJ AMY1_ORYSJ] Important for breakdown of endosperm starch during germination. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
AmyI-1 is an alpha-amylase from Oryza sativa (rice) and plays a crucial role in degrading starch in various tissues and at various growth stages. This enzyme is a glycoprotein with an N-glycosylated carbohydrate chain, a unique characteristic among plant alpha-amylases. In this study, we report the first crystal structure of AmyI-1 at 2.2-A resolution. The structure consists of a typical (beta/alpha)8-barrel, which is well-conserved among most alpha-amylases in the glycoside hydrolase family-13. Structural superimposition indicated small variations in the catalytic domain and carbohydrate-binding sites between AmyI-1 and barley alpha-amylases. By contrast, regions around the N-linked glycosylation sites displayed lower conservation of amino acid residues, including Asn-263, Asn-265, Thr-307, Asn-342, Pro-373, and Ala-374 in AmyI-1, which are not conserved in barley alpha-amylases, suggesting that these residues may contribute to the construction of the structure of glycosylated AmyI-1. These results increase the depths of our understanding of the biological functions of AmyI-1. | |||
Crystal structure of alpha-amylase from Oryza sativa: molecular insights into enzyme activity and thermostability.,Ochiai A, Sugai H, Harada K, Tanaka S, Ishiyama Y, Ito K, Tanaka T, Uchiumi T, Taniguchi M, Mitsui T Biosci Biotechnol Biochem. 2014;78(6):989-97. doi: 10.1080/09168451.2014.917261. , Epub 2014 Jun 18. PMID:25036124<ref>PMID:25036124</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3wn6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Amylase 3D structures|Amylase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Oryza sativa Japonica Group]] | |||
[[Category: Harada K]] | |||
[[Category: Ishiyama Y]] | |||
[[Category: Ito K]] | |||
[[Category: Mitsui T]] | |||
[[Category: Ochiai A]] | |||
[[Category: Sugai H]] | |||
[[Category: Tanaka S]] | |||
[[Category: Tanaka T]] | |||
[[Category: Taniguchi M]] | |||
[[Category: Uchiumi T]] | |||