OCA at 11:58, 1 February 2024

OCA — Thu, 01 Feb 2024 11:58:06 GMT

←Older revision		Revision as of 11:58, 1 February 2024
Line 1:		Line 1:

	==X-ray structure of mutated arabinofuranosidase==		==X-ray structure of mutated arabinofuranosidase==
-	<StructureSection load='6zt9' size='340' side='right'caption='[[6zt9]]' scene=''>	+	<StructureSection load='6zt9' size='340' side='right'caption='[[6zt9]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZT9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6zt9]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobacillus_xylanilyticus Thermobacillus xylanilyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZT9 FirstGlance]. <br>
-	</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=6zt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zt9 OCA], [https://pdbe.org/6zt9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zt9 RCSB], [https://www.ebi.ac.uk/pdbsum/6zt9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zt9 ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AHR:ALPHA-L-ARABINOFURANOSE'>AHR</scene>, <scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></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=6zt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zt9 OCA], [https://pdbe.org/6zt9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zt9 RCSB], [https://www.ebi.ac.uk/pdbsum/6zt9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zt9 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/O69262_THEXY O69262_THEXY]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The use of retaining glycoside hydrolases as synthetic tools for glycochemistry is highly topical and the focus of considerable research. However, due to the incomplete identification of the molecular determinants of the transglycosylation/hydrolysis partition (t/h), rational engineering of retaining glycoside hydrolases to create transglycosylases remains challenging. Therefore, to understand better the factors that underpin transglycosylation in a GH51 retaining alpha-l-arabinofuranosidase from Thermobacillus xylanilyticus, the investigation of this enzyme's active site was pursued. Specifically, the properties of two mutants, F26L and L352M, located in the vicinity of the active site are described, using kinetic and 3D structural analyses and molecular dynamics simulations. The results reveal that the presence of L352M in the context of a triple mutant (also containing R69H and N216W) generates changes both in the donor and acceptor subsites, the latter being the result of a domino-like effect. Overall, the mutant R69H-N216W-L352M displays excellent transglycosylation activity (70 % yield, 78 % transfer rate and reduced secondary hydrolysis of the product). In the course of this study, the central role played by the conserved R69 residue was also reaffirmed. The mutation R69H affects both the catalytic nucleophile and the acid/base, including their flexibility, and has a determinant effect on the t/h partition. Finally, the results reveal that increased loop flexibility in the acceptor subsites creates new interactions with the acceptor, in particular with a hydrophobic binding platform composed of N216W, W248 and W302.
		+
		+	Probing the determinants of the transglycosylation/hydrolysis partition in a retaining alpha-l-arabinofuranosidase.,Zhao J, Tandrup T, Bissaro B, Barbe S, Poulsen JN, Andre I, Dumon C, Lo Leggio L, O'Donohue MJ, Faure R N Biotechnol. 2021 May 25;62:68-78. doi: 10.1016/j.nbt.2021.01.008. Epub 2021 Jan , 29. PMID:33524585<ref>PMID:33524585</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6zt9" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
		+	[[Category: Thermobacillus xylanilyticus]]
	[[Category: Andre I]]		[[Category: Andre I]]
	[[Category: Barbe S]]		[[Category: Barbe S]]

OCA at 10:57, 10 February 2021

OCA — Wed, 10 Feb 2021 10:57:50 GMT

←Older revision		Revision as of 10:57, 10 February 2021
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6zt9 is ~~ON HOLD until Paper Publication~~	+	==X-ray structure of mutated arabinofuranosidase==
-		+	<StructureSection load='6zt9' size='340' side='right'caption='[[6zt9]]' scene=''>
-	~~Authors~~:	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZT9 FirstGlance]. <br>
-	~~Description~~:	+	</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=6zt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zt9 OCA], [https://pdbe.org/6zt9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zt9 RCSB], [https://www.ebi.ac.uk/pdbsum/6zt9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zt9 ProSAT]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Andre I]]
		+	[[Category: Barbe S]]
		+	[[Category: Bissaro B]]
		+	[[Category: Dumon C]]
		+	[[Category: Faure R]]
		+	[[Category: Lo Leggio L]]
		+	[[Category: O'Donohue MJ]]
		+	[[Category: Tandrup T]]
		+	[[Category: Zhao J]]

OCA at 04:35, 19 August 2020

OCA — Wed, 19 Aug 2020 04:35:05 GMT

←Older revision		Revision as of 04:35, 19 August 2020
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 6zt9 is ON HOLD	+	The entry 6zt9 is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "6zt9" [edit=sysop:move=sysop]

OCA — Wed, 29 Jul 2020 09:33:23 GMT

Protected "6zt9" [edit=sysop:move=sysop]

←Older revision

Revision as of 09:33, 29 July 2020

OCA: New page: '''Unreleased structure''' The entry 6zt9 is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 29 Jul 2020 09:33:21 GMT

New page: '''Unreleased structure''' The entry 6zt9 is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 6zt9 is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]

6zt9 - Revision history

OCA at 11:58, 1 February 2024

OCA at 10:57, 10 February 2021

OCA at 04:35, 19 August 2020

OCA: Protected "6zt9" [edit=sysop:move=sysop]

OCA: New page: '''Unreleased structure''' The entry 6zt9 is ON HOLD Authors: Description: Category: Unreleased Structures