8p5y - Revision history

OCA at 11:22, 14 March 2024

2024-03-14T11:22:02Z

←Older revision		Revision as of 11:22, 14 March 2024
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	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).		[https://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Artificial (transfer) hydrogenases have been developed for organic synthesis, but they rely on precious metals. Native hydrogenases use Earth-abundant metals, but these cannot be applied for organic synthesis due, in part, to their substrate specificity. Herein, we report the design and development of manganese transfer hydrogenases based on the biotin-streptavidin technology. By incorporating bio-mimetic Mn(I) complexes into the binding cavity of streptavidin, and through chemo-genetic optimization, we have obtained artificial enzymes that hydrogenate ketones with nearly quantitative yield and up to 98 % enantiomeric excess (ee). These enzymes exhibit broad substrate scope and high functional-group tolerance. According to QM/MM calculations and X-ray crystallography, the S112Y mutation, combined with the appropriate chemical structure of the Mn cofactor plays a critical role in the reactivity and enantioselectivity of the artificial metalloenzyme (ArMs). Our work highlights the potential of ArMs incorporating base-meal cofactors for enantioselective organic synthesis.
-
-	Manganese Transfer Hydrogenases Based on the Biotin-Streptavidin Technology.,Wang W, Tachibana R, Zou Z, Chen D, Zhang X, Lau K, Pojer F, Ward TR, Hu X Angew Chem Int Ed Engl. 2023 Oct 23;62(43):e202311896. doi: , 10.1002/anie.202311896. Epub 2023 Sep 18. PMID:37671593<ref>PMID:37671593</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 8p5y" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 10:36, 25 October 2023

2023-10-25T10:36:13Z

←Older revision		Revision as of 10:36, 25 October 2023
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-	'''Unreleased structure'''

-	~~The entry~~ 8p5y is ~~ON HOLD until Paper~~ Publication	+	==Artificial transfer hydrogenase with a Mn-12 cofactor and Streptavidin S112Y-K121M mutant==
		+	<StructureSection load='8p5y' size='340' side='right'caption='[[8p5y]], [[Resolution\|resolution]] 1.88Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8p5y]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_avidinii Streptomyces avidinii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8P5Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8P5Y 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]] 1.88Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=WZQ:5-[(3~{a}~{S},4~{S},6~{a}~{R})-2-oxidanylidene-1,3,3~{a},4,6,6~{a}-hexahydrothieno[3,4-d]imidazol-4-yl]-~{N}-[2-(3,4-dihydro-2~{H}-pyrano[2,3-c]pyridin-6-ylmethylamino)ethyl]pentanamide'>WZQ</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=8p5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8p5y OCA], [https://pdbe.org/8p5y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8p5y RCSB], [https://www.ebi.ac.uk/pdbsum/8p5y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8p5y ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/SAV_STRAV SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Artificial (transfer) hydrogenases have been developed for organic synthesis, but they rely on precious metals. Native hydrogenases use Earth-abundant metals, but these cannot be applied for organic synthesis due, in part, to their substrate specificity. Herein, we report the design and development of manganese transfer hydrogenases based on the biotin-streptavidin technology. By incorporating bio-mimetic Mn(I) complexes into the binding cavity of streptavidin, and through chemo-genetic optimization, we have obtained artificial enzymes that hydrogenate ketones with nearly quantitative yield and up to 98 % enantiomeric excess (ee). These enzymes exhibit broad substrate scope and high functional-group tolerance. According to QM/MM calculations and X-ray crystallography, the S112Y mutation, combined with the appropriate chemical structure of the Mn cofactor plays a critical role in the reactivity and enantioselectivity of the artificial metalloenzyme (ArMs). Our work highlights the potential of ArMs incorporating base-meal cofactors for enantioselective organic synthesis.

-	~~Authors: Lau, K~~., Wang, W., ~~Pojer~~, F., ~~Larabi~~, A.	+	Manganese Transfer Hydrogenases Based on the Biotin-Streptavidin Technology.,Wang W, Tachibana R, Zou Z, Chen D, Zhang X, Lau K, Pojer F, Ward TR, Hu X Angew Chem Int Ed Engl. 2023 Oct 23;62(43):e202311896. doi: , 10.1002/anie.202311896. Epub 2023 Sep 18. PMID:37671593<ref>PMID:37671593</ref>

-	~~Description: Artificial transfer hydrogenase with~~ a Mn-~~12 cofactor and Streptavidin S112Y~~-~~K121M mutant~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
-	[[Category: ~~Wang, W~~]]	+	<div class="pdbe-citations 8p5y" style="background-color:#fffaf0;"></div>
-	[[Category: ~~Pojer, F~~]]	+	== References ==
-	[[Category: ~~Larabi, A~~]]	+	<references/>
-	[[Category: ~~Lau, K~~]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Streptomyces avidinii]]
		+	[[Category: Larabi A]]
		+	[[Category: Lau K]]
		+	[[Category: Pojer F]]
		+	[[Category: Wang W]]

OCA at 19:48, 28 June 2023

2023-06-28T19:48:18Z

←Older revision		Revision as of 19:48, 28 June 2023
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 8p5y is ON HOLD	+	The entry 8p5y is ON HOLD until Paper Publication

	Authors: Lau, K., Wang, W., Pojer, F., Larabi, A.		Authors: Lau, K., Wang, W., Pojer, F., Larabi, A.

OCA: Protected "8p5y" [edit=sysop:move=sysop]

2023-05-31T04:10:08Z

Protected "8p5y" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:10, 31 May 2023

OCA: New page: '''Unreleased structure''' The entry 8p5y is ON HOLD Authors: Lau, K., Wang, W., Pojer, F., Larabi, A. Description: Artificial transfer hydrogenase with a Mn-12 cofactor and Streptavid...

2023-05-31T04:10:07Z

New page: '''Unreleased structure''' The entry 8p5y is ON HOLD Authors: Lau, K., Wang, W., Pojer, F., Larabi, A. Description: Artificial transfer hydrogenase with a Mn-12 cofactor and Streptavid...

New page

'''Unreleased structure'''

The entry 8p5y is ON HOLD

Authors: Lau, K., Wang, W., Pojer, F., Larabi, A.

Description: Artificial transfer hydrogenase with a Mn-12 cofactor and Streptavidin S112Y-K121M mutant
[[Category: Unreleased Structures]]
[[Category: Wang, W]]
[[Category: Pojer, F]]
[[Category: Larabi, A]]
[[Category: Lau, K]]