4aef: Difference between revisions

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~~'''Unreleased structure'''~~

The ~~entry 4aef~~ is ~~ON HOLD~~

==THE CRYSTAL STRUCTURE OF THERMOSTABLE AMYLASE FROM THE PYROCOCCUS==

== 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]] 2.34Å</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]

== 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.

~~Authors: SONG, H.~~-N., ~~JUNG~~, T.-Y.~~, YOON, S~~.-M.~~, YANG, S~~.-J.~~, PARK, K~~.-H., ~~WOO, E.-J~~.

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>

~~Description~~: ~~THE CRYSTAL STRUCTURE OF THERMOSTABLE AMYLASE FROM THE PYROCOCCUS~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

==See Also==

*[[Amylase 3D structures|Amylase 3D structures]]

== 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]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4aef is ON HOLD
+==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.
-Authors: SONG, H.-N., JUNG, T.-Y., YOON, S.-M., YANG, S.-J., PARK, K.-H., WOO, E.-J.
+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>
-Description: THE CRYSTAL STRUCTURE OF THERMOSTABLE AMYLASE FROM THE PYROCOCCUS
+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]]