3wn6: Difference between revisions
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''' | ==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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WN6 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><br> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wn6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wn6 RCSB], [http://www.ebi.ac.uk/pdbsum/3wn6 PDBsum]</span></td></tr> | |||
<table> | |||
<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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Alpha-amylase]] | |||
[[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.]] | |||
[[Category: Carbohydrate/sugar binding]] | |||
[[Category: Glycosylation]] | |||
[[Category: Hydrolase]] | |||
