4ays: Difference between revisions
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The | ==The Structure of Amylosucrase from D. radiodurans== | ||
<StructureSection load='4ays' size='340' side='right'caption='[[4ays]], [[Resolution|resolution]] 3.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ays]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AYS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AYS 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]] 3.15Å</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=4ays FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ays OCA], [https://pdbe.org/4ays PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ays RCSB], [https://www.ebi.ac.uk/pdbsum/4ays PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ays ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9RVT9_DEIRA Q9RVT9_DEIRA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Amylosucrases (ASes) catalyze the formation of an alpha-1,4-glucosidic linkage by transferring a glucosyl unit from sucrose onto an acceptor alpha-1,4-glucan. To date, several ligand-bound crystal structures of wild-type and mutant ASes from Neisseria polysaccharea and Deinococcus geothermalis have been solved. These structures all display a very similar overall conformation with a deep pocket leading to the site for transglucosylation, subsite -1. This has led to speculation on how sucrose enters the active site during glucan elongation. In contrast to previous studies, the AS structure from D. radiodurans presented here has a completely empty -1 subsite. This structure is strikingly different from other AS structures, as an active-site-lining loop comprising residues Leu214-Asn225 is found in a previously unobserved conformation. In addition, a large loop harbouring the conserved active-site residues Asp133 and Tyr136 is disordered. The result of the changed loop conformations is that the active-site topology is radically changed, leaving subsite -1 exposed and partially dismantled. This structure provides novel insights into the dynamics of ASes and comprises the first structural support for an elongation mechanism that involves considerable conformational changes to modulate accessibility to the sucrose-binding site and thereby allows successive cycles of glucosyl-moiety transfer to a growing glucan chain. | |||
The structure of amylosucrase from Deinococcus radiodurans has an unusual open active-site topology.,Skov LK, Pizzut-Serin S, Remaud-Simeon M, Ernst HA, Gajhede M, Mirza O Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Sep;69(Pt 9):973-8. doi:, 10.1107/S1744309113021714. Epub 2013 Aug 19. PMID:23989143<ref>PMID:23989143</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4ays" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Amylase 3D structures|Amylase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Deinococcus radiodurans]] | |||
[[Category: Large Structures]] | |||
[[Category: Gajhede M]] | |||
[[Category: Mirza O]] | |||
[[Category: Pizzut S]] | |||
[[Category: Remaud-Simeon M]] | |||
[[Category: Skov LK]] | |||
Latest revision as of 14:38, 20 December 2023
The Structure of Amylosucrase from D. radioduransThe Structure of Amylosucrase from D. radiodurans
Structural highlights
FunctionPublication Abstract from PubMedAmylosucrases (ASes) catalyze the formation of an alpha-1,4-glucosidic linkage by transferring a glucosyl unit from sucrose onto an acceptor alpha-1,4-glucan. To date, several ligand-bound crystal structures of wild-type and mutant ASes from Neisseria polysaccharea and Deinococcus geothermalis have been solved. These structures all display a very similar overall conformation with a deep pocket leading to the site for transglucosylation, subsite -1. This has led to speculation on how sucrose enters the active site during glucan elongation. In contrast to previous studies, the AS structure from D. radiodurans presented here has a completely empty -1 subsite. This structure is strikingly different from other AS structures, as an active-site-lining loop comprising residues Leu214-Asn225 is found in a previously unobserved conformation. In addition, a large loop harbouring the conserved active-site residues Asp133 and Tyr136 is disordered. The result of the changed loop conformations is that the active-site topology is radically changed, leaving subsite -1 exposed and partially dismantled. This structure provides novel insights into the dynamics of ASes and comprises the first structural support for an elongation mechanism that involves considerable conformational changes to modulate accessibility to the sucrose-binding site and thereby allows successive cycles of glucosyl-moiety transfer to a growing glucan chain. The structure of amylosucrase from Deinococcus radiodurans has an unusual open active-site topology.,Skov LK, Pizzut-Serin S, Remaud-Simeon M, Ernst HA, Gajhede M, Mirza O Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Sep;69(Pt 9):973-8. doi:, 10.1107/S1744309113021714. Epub 2013 Aug 19. PMID:23989143[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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