7tuv - Revision history

OCA at 07:22, 3 April 2024

OCA — Wed, 03 Apr 2024 07:22:02 GMT

←Older revision		Revision as of 07:22, 3 April 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[7tuv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TUV FirstGlance]. <br>		<table><tr><td colspan='2'>[[7tuv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TUV FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</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]] 2.225Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</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=7tuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tuv OCA], [https://pdbe.org/7tuv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tuv RCSB], [https://www.ebi.ac.uk/pdbsum/7tuv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tuv 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=7tuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tuv OCA], [https://pdbe.org/7tuv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tuv RCSB], [https://www.ebi.ac.uk/pdbsum/7tuv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tuv ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/Q95Z12_9TRYP Q95Z12_9TRYP]		[https://www.uniprot.org/uniprot/Q95Z12_9TRYP Q95Z12_9TRYP]
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Rrp44/Dis3 is a conserved eukaryotic ribonuclease that acts on processing and degradation of nearly all types of RNA. It contains an endo- (PIN) and an exonucleolytic (RNB) domain and, its depletion in model organisms supports its essential function for cell viability. In Trypanosoma brucei, depletion of Rrp44 (TbRRP44) blocks maturation of ribosomal RNA, leading to disruption of ribosome synthesis and inhibition of cell proliferation. We have determined the crystal structure of the exoribonucleolytic module of TbRRP44 in an active conformation, revealing novel details of the catalytic mechanism of the RNB domain. For the first time, the position of the second magnesium involved in the two-metal-ion mechanism was determined for a member of the RNase II family. In vitro, TbRRP44 acts preferentially on non-structured uridine-rich RNA substrates. However, we demonstrated for the first time that both TbRRP44 and its homologue from Saccharomyces cerevisiae can also degrade structured substrates without 3'-end overhang, suggesting that Rrp44/Dis3 ribonucleases may be involved in degradation of a wider panel of RNA than has been assumed. Interestingly, deletion of TbRRP44 PIN domain impairs RNA binding to different extents, depending on the type of substrate.

-	Trypanosoma brucei RRP44: a versatile enzyme for processing structured and non-structured RNA substrates.,Cesaro G, da Soler HT, Guerra-Slompo EP, Haouz A, Legrand P, Zanchin NIT, Guimaraes BG Nucleic Acids Res. 2022 Dec 30:gkac1199. doi: 10.1093/nar/gkac1199. PMID:36583334<ref>PMID:36583334</ref>	+	==See Also==
-		+	*[[Ribonuclease 3D structures\|Ribonuclease 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 7tuv" style="background-color:#fffaf0;"></div>~~	+
-	== ~~References~~ ==	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 07:33, 11 January 2023

OCA — Wed, 11 Jan 2023 07:33:30 GMT

←Older revision		Revision as of 07:33, 11 January 2023
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 7tuv is ~~ON HOLD~~	+	==Crystal structure of the exoribonucleolytic module of T. brucei RRP44==
		+	<StructureSection load='7tuv' size='340' side='right'caption='[[7tuv]], [[Resolution\|resolution]] 2.23Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[7tuv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7TUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7TUV FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</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=7tuv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7tuv OCA], [https://pdbe.org/7tuv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7tuv RCSB], [https://www.ebi.ac.uk/pdbsum/7tuv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7tuv ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/Q95Z12_9TRYP Q95Z12_9TRYP]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Rrp44/Dis3 is a conserved eukaryotic ribonuclease that acts on processing and degradation of nearly all types of RNA. It contains an endo- (PIN) and an exonucleolytic (RNB) domain and, its depletion in model organisms supports its essential function for cell viability. In Trypanosoma brucei, depletion of Rrp44 (TbRRP44) blocks maturation of ribosomal RNA, leading to disruption of ribosome synthesis and inhibition of cell proliferation. We have determined the crystal structure of the exoribonucleolytic module of TbRRP44 in an active conformation, revealing novel details of the catalytic mechanism of the RNB domain. For the first time, the position of the second magnesium involved in the two-metal-ion mechanism was determined for a member of the RNase II family. In vitro, TbRRP44 acts preferentially on non-structured uridine-rich RNA substrates. However, we demonstrated for the first time that both TbRRP44 and its homologue from Saccharomyces cerevisiae can also degrade structured substrates without 3'-end overhang, suggesting that Rrp44/Dis3 ribonucleases may be involved in degradation of a wider panel of RNA than has been assumed. Interestingly, deletion of TbRRP44 PIN domain impairs RNA binding to different extents, depending on the type of substrate.

-	~~Authors~~: ~~Cesaro~~, G., ~~Guimaraes~~, B.G.	+	Trypanosoma brucei RRP44: a versatile enzyme for processing structured and non-structured RNA substrates.,Cesaro G, da Soler HT, Guerra-Slompo EP, Haouz A, Legrand P, Zanchin NIT, Guimaraes BG Nucleic Acids Res. 2022 Dec 30:gkac1199. doi: 10.1093/nar/gkac1199. PMID:36583334<ref>PMID:36583334</ref>

-	~~Description: Crystal structure~~ of the ~~exoribonucleolytic module~~ of T. ~~brucei RRP44~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased~~ Structures]]	+	</div>
-	[[Category: ~~Guimaraes, B.G~~]]	+	<div class="pdbe-citations 7tuv" style="background-color:#fffaf0;"></div>
-	[[Category: Cesaro, G]]	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Synthetic construct]]
		+	[[Category: Trypanosoma brucei]]
		+	[[Category: Cesaro G]]
		+	[[Category: Guimaraes BG]]

OCA: Protected "7tuv" [edit=sysop:move=sysop]

OCA — Wed, 09 Feb 2022 06:23:18 GMT

Protected "7tuv" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:23, 9 February 2022

OCA: New page: '''Unreleased structure''' The entry 7tuv is ON HOLD Authors: Cesaro, G., Guimaraes, B.G. Description: Crystal structure of the exoribonucleolytic module of T. brucei RRP44 [[Category:...

OCA — Wed, 09 Feb 2022 06:23:17 GMT

New page: '''Unreleased structure''' The entry 7tuv is ON HOLD Authors: Cesaro, G., Guimaraes, B.G. Description: Crystal structure of the exoribonucleolytic module of T. brucei RRP44 [[Category:...

New page

'''Unreleased structure'''

The entry 7tuv is ON HOLD

Authors: Cesaro, G., Guimaraes, B.G.

Description: Crystal structure of the exoribonucleolytic module of T. brucei RRP44
[[Category: Unreleased Structures]]
[[Category: Guimaraes, B.G]]
[[Category: Cesaro, G]]