View source for 4aef


==THE CRYSTAL STRUCTURE OF THERMOSTABLE AMYLASE FROM THE PYROCOCCUS==
<StructureSection load='4aef' size='340' side='right'caption='[[4aef]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4aef]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AEF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AEF 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]] 2.34&#8491;</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=4aef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aef OCA], [https://pdbe.org/4aef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aef RCSB], [https://www.ebi.ac.uk/pdbsum/4aef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aef ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8TZP8_PYRFU Q8TZP8_PYRFU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
PFTA (Pyrococcus furiosus thermostable amylase) is a hyperthermophilic amylase isolated from the archaeon Pyrococcus furiosus. This enzyme possesses characteristics of both alpha-amylase- and cyclodextrin (CD)-hydrolyzing enzymes, allowing it to degrade pullulan, CD and acarbose-activities that are absent in most alpha-amylases-without the transferring activity that is common in CD-hydrolyzing enzymes. The crystal structure of PFTA revealed a unique monomeric subunit with an extended N-terminal region and an N'-domain folded into its own active site-a significantly altered domain configuration relative to that of the conventional dimeric CD-hydrolyzing amylases in glycoside hydrolase family 13. The active site is formed by the interface of the N'-domain and the catalytic domain and exhibits a broad and wide-open geometry without the concave pocket that is commonly found in the active sites of maltogenic amylases. The mutation of a residue (Gly415 to Glu) located at the domain interface between the N'- and catalytic domains yielded an enzyme that produced a significantly higher purity maltoheptaose (G7) from beta-CD, supporting the involvement of this interface in substrate recognition and indicating that this mutant enzyme is a suitable candidate for the production of pure G7. The unique configuration of the active site distinguishes this archaic monomeric enzyme from classical bacterial CD-hydrolyzing amylases and provides a molecular basis for its enzymatic characteristics and for its potential use in industrial applications.

A novel domain arrangement in a monomeric cyclodextrin-hydrolyzing enzyme from the hyperthermophile Pyrococcus furiosus.,Park JT, Song HN, Jung TY, Lee MH, Park SG, Woo EJ, Park KH Biochim Biophys Acta. 2013 Jan;1834(1):380-6. doi: 10.1016/j.bbapap.2012.08.001. , Epub 2012 Aug 8. PMID:22902546<ref>PMID:22902546</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4aef" style="background-color:#fffaf0;"></div>

==See Also==
*[[Amylase 3D structures|Amylase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus furiosus]]
[[Category: Jung T-Y]]
[[Category: Park K-H]]
[[Category: Song H-N]]
[[Category: Woo E-J]]
[[Category: Yang S-J]]
[[Category: Yoon S-M]]