4aee: Difference between revisions
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<StructureSection load='4aee' size='340' side='right'caption='[[4aee]], [[Resolution|resolution]] 2.28Å' scene=''> | <StructureSection load='4aee' size='340' side='right'caption='[[4aee]], [[Resolution|resolution]] 2.28Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4aee]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4aee]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43588 Atcc 43588]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AEE FirstGlance]. <br> | ||
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glucan_1,4-alpha-maltohydrolase Glucan 1,4-alpha-maltohydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.133 3.2.1.133] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4aee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aee OCA], [https://pdbe.org/4aee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aee RCSB], [https://www.ebi.ac.uk/pdbsum/4aee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aee ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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==See Also== | ==See Also== | ||
*[[Amylase|Amylase]] | *[[Amylase 3D structures|Amylase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Atcc 43588]] | [[Category: Atcc 43588]] | ||
[[Category: Glucan 1,4-alpha-maltohydrolase]] | [[Category: Glucan 1,4-alpha-maltohydrolase]] | ||
[[Category: Large Structures]] | |||
[[Category: Jung, T Y]] | [[Category: Jung, T Y]] | ||
[[Category: Park, C H]] | [[Category: Park, C H]] | ||
Revision as of 08:31, 25 August 2022
CRYSTAL STRUCTURE OF MALTOGENIC AMYLASE FROM S.MARINUSCRYSTAL STRUCTURE OF MALTOGENIC AMYLASE FROM S.MARINUS
Structural highlights
Publication Abstract from PubMedStaphylothermus marinus maltogenic amylase (SMMA) is a novel extreme thermophile maltogenic amylase with an optimal temperature of 100 degrees C, which hydrolyzes alpha-(1-4)-glycosyl linkages in cyclodextrins and in linear malto-oligosaccharides. This enzyme has a long N-terminal extension that is conserved among archaic hyperthermophilic amylases but is not found in other hydrolyzing enzymes from the glycoside hydrolase 13 family. The SMMA crystal structure revealed that the N-terminal extension forms an N' domain that is similar to carbohydrate-binding module 48, with the strand-loop-strand region forming a part of the substrate binding pocket with several aromatic residues, including Phe-95, Phe-96, and Tyr-99. A structural comparison with conventional cyclodextrin-hydrolyzing enzymes revealed a striking resemblance between the SMMA N' domain position and the dimeric N domain position in bacterial enzymes. This result suggests that extremophilic archaea that live at high temperatures may have adopted a novel domain arrangement that combines all of the substrate binding components within a monomeric subunit. The SMMA structure provides a molecular basis for the functional properties that are unique to hyperthermophile maltogenic amylases from archaea and that distinguish SMMA from moderate thermophilic or mesophilic bacterial enzymes. Association of Novel Domain in Active Site of Archaic Hyperthermophilic Maltogenic Amylase from Staphylothermus marinus.,Jung TY, Li D, Park JT, Yoon SM, Tran PL, Oh BH, Janecek S, Park SG, Woo EJ, Park KH J Biol Chem. 2012 Mar 9;287(11):7979-89. Epub 2012 Jan 5. PMID:22223643[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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