8asu - Revision history

OCA at 08:13, 7 February 2024

OCA — Wed, 07 Feb 2024 08:13:34 GMT

←Older revision		Revision as of 08:13, 7 February 2024
Line 10:		Line 10:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/A0A0N1ABZ3_9HYPH A0A0N1ABZ3_9HYPH]		[https://www.uniprot.org/uniprot/A0A0N1ABZ3_9HYPH A0A0N1ABZ3_9HYPH]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The dimeric avidin family has been expanded in recent years to include many new members. All of them lack the intermonomeric Trp that plays a critical role in biotin-binding. Nevertheless, these new members of the avidins maintain the high affinity towards biotin. Additionally, all of the dimeric avidins share a very unique property: namely, the cylindrical oligomerization in the crystal structure. The newest member described here, agroavidin from the agrobacterium, Rhizobium sp. AAP43, shares their important structural features. However, the affinity of agroavidin towards biotin is lower than all other members of the avidin family, due to the presence of phenylalanine instead of a conserved tyrosine in the biotin-binding site. Mutating this phenylalanine into tyrosine regenerated the high affinity, which emphasizes the importance of this particular tyrosine residue. Another unique feature that distinguishes agroavidin from the other dimeric avidins is that it does not produce oligomers in its crystal structure. In order to understand the factors that promote oligomerization in dimeric avidins, we exchanged the C-terminal region of agroavidin with that of hoefavidin that produced octamers. This exchange resulted in a decamer rather than an octamer. This unusual outcome demonstrates the impact of the C-terminal region on the ability to produce oligomers. The decameric assembly of agroavidin expands the avidin-biotin toolbox even further and could well pave the path into new biotin-based technologies. Moreover, uncovering the factors that induce dimeric avidins into oligomeric assemblies may aid in better understanding the general molecular determinants that promote oligomerization.
-
-	Self-assembly of a dimeric avidin into unique higher-order oligomers.,Bana J, Warwar J, Bayer EA, Livnah O FEBS J. 2023 Feb 28. doi: 10.1111/febs.16764. PMID:36853192<ref>PMID:36853192</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 8asu" style="background-color:#fffaf0;"></div>
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 11:10, 2 August 2023

OCA — Wed, 02 Aug 2023 11:10:27 GMT

←Older revision		Revision as of 11:10, 2 August 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[8asu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizobium_sp._AAP43 Rhizobium sp. AAP43]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ASU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ASU FirstGlance]. <br>		<table><tr><td colspan='2'>[[8asu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizobium_sp._AAP43 Rhizobium sp. AAP43]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ASU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ASU FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene></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]] 2.52Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</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=8asu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8asu OCA], [https://pdbe.org/8asu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8asu RCSB], [https://www.ebi.ac.uk/pdbsum/8asu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8asu ProSAT]</span></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=8asu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8asu OCA], [https://pdbe.org/8asu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8asu RCSB], [https://www.ebi.ac.uk/pdbsum/8asu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8asu ProSAT]</span></td></tr>
	</table>		</table>

OCA at 20:29, 12 April 2023

OCA — Wed, 12 Apr 2023 20:29:58 GMT

←Older revision		Revision as of 20:29, 12 April 2023
Line 1:		Line 1:
-	'''Unreleased structure'''

-	The ~~entry~~ 8asu is ~~ON HOLD~~	+	==The Crystal structure of short F46Y agroavidin - biotin complex==
		+	<StructureSection load='8asu' size='340' side='right'caption='[[8asu]], [[Resolution\|resolution]] 2.52Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[8asu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhizobium_sp._AAP43 Rhizobium sp. AAP43]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ASU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ASU FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</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=8asu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8asu OCA], [https://pdbe.org/8asu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8asu RCSB], [https://www.ebi.ac.uk/pdbsum/8asu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8asu ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/A0A0N1ABZ3_9HYPH A0A0N1ABZ3_9HYPH]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The dimeric avidin family has been expanded in recent years to include many new members. All of them lack the intermonomeric Trp that plays a critical role in biotin-binding. Nevertheless, these new members of the avidins maintain the high affinity towards biotin. Additionally, all of the dimeric avidins share a very unique property: namely, the cylindrical oligomerization in the crystal structure. The newest member described here, agroavidin from the agrobacterium, Rhizobium sp. AAP43, shares their important structural features. However, the affinity of agroavidin towards biotin is lower than all other members of the avidin family, due to the presence of phenylalanine instead of a conserved tyrosine in the biotin-binding site. Mutating this phenylalanine into tyrosine regenerated the high affinity, which emphasizes the importance of this particular tyrosine residue. Another unique feature that distinguishes agroavidin from the other dimeric avidins is that it does not produce oligomers in its crystal structure. In order to understand the factors that promote oligomerization in dimeric avidins, we exchanged the C-terminal region of agroavidin with that of hoefavidin that produced octamers. This exchange resulted in a decamer rather than an octamer. This unusual outcome demonstrates the impact of the C-terminal region on the ability to produce oligomers. The decameric assembly of agroavidin expands the avidin-biotin toolbox even further and could well pave the path into new biotin-based technologies. Moreover, uncovering the factors that induce dimeric avidins into oligomeric assemblies may aid in better understanding the general molecular determinants that promote oligomerization.

-	~~Authors~~:	+	Self-assembly of a dimeric avidin into unique higher-order oligomers.,Bana J, Warwar J, Bayer EA, Livnah O FEBS J. 2023 Feb 28. doi: 10.1111/febs.16764. PMID:36853192<ref>PMID:36853192</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
		+	<div class="pdbe-citations 8asu" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Rhizobium sp. AAP43]]
		+	[[Category: Bana J]]
		+	[[Category: Livnah O]]

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

OCA — Wed, 31 Aug 2022 05:26:08 GMT

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

←Older revision

Revision as of 05:26, 31 August 2022

OCA: New page: '''Unreleased structure''' The entry 8asu is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 31 Aug 2022 05:26:07 GMT

New page: '''Unreleased structure''' The entry 8asu is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 8asu is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]