5xjl - Revision history

OCA at 10:18, 27 March 2024

OCA — Wed, 27 Mar 2024 10:18:50 GMT

←Older revision		Revision as of 10:18, 27 March 2024
Line 3:		Line 3:
	<StructureSection load='5xjl' size='340' side='right'caption='[[5xjl]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='5xjl' size='340' side='right'caption='[[5xjl]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5xjl]] is a 7 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3s6n 3s6n]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XJL OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=5XJL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5xjl]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3s6n 3s6n]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XJL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XJL FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=5xjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xjl OCA], [~~http~~://pdbe.org/5xjl PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5xjl RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5xjl PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5xjl 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]] 2.5Å</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=5xjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xjl OCA], [https://pdbe.org/5xjl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xjl RCSB], [https://www.ebi.ac.uk/pdbsum/5xjl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xjl ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/RUXG_HUMAN RUXG_HUMAN]] Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing. Associated with snRNP U1, U2, U4/U6 and U5. [[http://www.uniprot.org/uniprot/RUXE_HUMAN RUXE_HUMAN]] Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing. Associated with snRNP U1, U2, U4/U6 and U5. [[http://www.uniprot.org/uniprot/GEMI2_HUMAN GEMI2_HUMAN]] The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus.<ref>PMID:18984161</ref> <ref>PMID:9323129</ref> [[http://www.uniprot.org/uniprot/SMD2_HUMAN SMD2_HUMAN]] Required for pre-mRNA splicing. Required for snRNP biogenesis (By similarity). [[http://www.uniprot.org/uniprot/SMD1_HUMAN SMD1_HUMAN]] May act as a charged protein scaffold to promote snRNP assembly or strengthen snRNP-snRNP interactions through nonspecific electrostatic contacts with RNA. [[http://www.uniprot.org/uniprot/RUXF_HUMAN RUXF_HUMAN]] Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing. Associated with snRNP U1, U2, U4/U6 and U5.	+	[https://www.uniprot.org/uniprot/GEMI2_HUMAN GEMI2_HUMAN] The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus.<ref>PMID:18984161</ref> <ref>PMID:9323129</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	The SMN complex mediates the assembly of heptameric Sm protein rings on small nuclear RNAs (snRNAs), which are essential for snRNP function. Specific Sm core assembly depends on Sm proteins and snRNA recognition by SMN/Gemin2- and Gemin5-containing subunits, respectively. The mechanism by which the Sm proteins are gathered while preventing illicit Sm assembly on non-snRNAs is unknown. Here, we describe the 2.5 A crystal structure of Gemin2 bound to SmD1/D2/F/E/G pentamer and SMN's Gemin2-binding domain, a key assembly intermediate. Remarkably, through its extended conformation, Gemin2 wraps around the crescent-shaped pentamer, interacting with all five Sm proteins, and gripping its bottom and top sides and outer perimeter. Gemin2 reaches into the RNA-binding pocket, preventing RNA binding. Interestingly, SMN-Gemin2 interaction is abrogated by a spinal muscular atrophy (SMA)-causing mutation in an SMN helix that mediates Gemin2 binding. These findings provide insight into SMN complex assembly and specificity, linking snRNP biogenesis and SMA pathogenesis.	+
-		+
-	Structure of a Key Intermediate of the SMN Complex Reveals Gemin2's Crucial Function in snRNP Assembly.,Zhang R, So BR, Li P, Yong J, Glisovic T, Wan L, Dreyfuss G Cell. 2011 Aug 5;146(3):384-95. PMID:21816274<ref>PMID:21816274</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 5xjl" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
	*[[Nucleoprotein 3D structures\|Nucleoprotein 3D structures]]		*[[Nucleoprotein 3D structures\|Nucleoprotein 3D structures]]
		+	*[[Sm-like protein 3D structures\|Sm-like protein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Zhang, R]]	+	[[Category: Zhang R]]
-	~~[[Category: Splicing~~]]	+

OCA at 06:51, 14 October 2020

OCA — Wed, 14 Oct 2020 06:51:54 GMT

←Older revision		Revision as of 06:51, 14 October 2020
Line 1:		Line 1:

	==Crystal Structure of the Gemin2-binding domain of SMN, Gemin2 in Complex with SmD1/D2/F/E/G from Human==		==Crystal Structure of the Gemin2-binding domain of SMN, Gemin2 in Complex with SmD1/D2/F/E/G from Human==
-	<StructureSection load='5xjl' size='340' side='right' caption='[[5xjl]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='5xjl' size='340' side='right'caption='[[5xjl]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5xjl]] is a 7 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3s6n 3s6n]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XJL OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5XJL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5xjl]] is a 7 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3s6n 3s6n]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XJL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XJL FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5xjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xjl OCA], [http://pdbe.org/5xjl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xjl RCSB], [http://www.ebi.ac.uk/pdbsum/5xjl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xjl ProSAT]</span></td></tr>	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5xjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xjl OCA], [http://pdbe.org/5xjl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xjl RCSB], [http://www.ebi.ac.uk/pdbsum/5xjl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xjl ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 17:
	</div>		</div>
	<div class="pdbe-citations 5xjl" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5xjl" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Nucleoprotein 3D structures\|Nucleoprotein 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Zhang, R]]		[[Category: Zhang, R]]
	[[Category: Splicing]]		[[Category: Splicing]]

OCA at 07:53, 2 May 2018

OCA — Wed, 02 May 2018 07:53:59 GMT

←Older revision		Revision as of 07:53, 2 May 2018
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The~~ entry 5xjl is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Crystal Structure of the Gemin2-binding domain of SMN, Gemin2 in Complex with SmD1/D2/F/E/G from Human==
		+	<StructureSection load='5xjl' size='340' side='right' caption='[[5xjl]], [[Resolution\|resolution]] 2.50Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[5xjl]] is a 7 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3s6n 3s6n]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XJL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XJL FirstGlance]. <br>
		+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5xjl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xjl OCA], [http://pdbe.org/5xjl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xjl RCSB], [http://www.ebi.ac.uk/pdbsum/5xjl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xjl ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/RUXG_HUMAN RUXG_HUMAN]] Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing. Associated with snRNP U1, U2, U4/U6 and U5. [[http://www.uniprot.org/uniprot/RUXE_HUMAN RUXE_HUMAN]] Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing. Associated with snRNP U1, U2, U4/U6 and U5. [[http://www.uniprot.org/uniprot/GEMI2_HUMAN GEMI2_HUMAN]] The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus.<ref>PMID:18984161</ref> <ref>PMID:9323129</ref> [[http://www.uniprot.org/uniprot/SMD2_HUMAN SMD2_HUMAN]] Required for pre-mRNA splicing. Required for snRNP biogenesis (By similarity). [[http://www.uniprot.org/uniprot/SMD1_HUMAN SMD1_HUMAN]] May act as a charged protein scaffold to promote snRNP assembly or strengthen snRNP-snRNP interactions through nonspecific electrostatic contacts with RNA. [[http://www.uniprot.org/uniprot/RUXF_HUMAN RUXF_HUMAN]] Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing. Associated with snRNP U1, U2, U4/U6 and U5.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The SMN complex mediates the assembly of heptameric Sm protein rings on small nuclear RNAs (snRNAs), which are essential for snRNP function. Specific Sm core assembly depends on Sm proteins and snRNA recognition by SMN/Gemin2- and Gemin5-containing subunits, respectively. The mechanism by which the Sm proteins are gathered while preventing illicit Sm assembly on non-snRNAs is unknown. Here, we describe the 2.5 A crystal structure of Gemin2 bound to SmD1/D2/F/E/G pentamer and SMN's Gemin2-binding domain, a key assembly intermediate. Remarkably, through its extended conformation, Gemin2 wraps around the crescent-shaped pentamer, interacting with all five Sm proteins, and gripping its bottom and top sides and outer perimeter. Gemin2 reaches into the RNA-binding pocket, preventing RNA binding. Interestingly, SMN-Gemin2 interaction is abrogated by a spinal muscular atrophy (SMA)-causing mutation in an SMN helix that mediates Gemin2 binding. These findings provide insight into SMN complex assembly and specificity, linking snRNP biogenesis and SMA pathogenesis.

-	~~Authors~~:	+	Structure of a Key Intermediate of the SMN Complex Reveals Gemin2's Crucial Function in snRNP Assembly.,Zhang R, So BR, Li P, Yong J, Glisovic T, Wan L, Dreyfuss G Cell. 2011 Aug 5;146(3):384-95. PMID:21816274<ref>PMID:21816274</ref>

-	~~Description~~:	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	[[Category: ~~Unreleased Structures~~]]	+	</div>
		+	<div class="pdbe-citations 5xjl" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Zhang, R]]
		+	[[Category: Splicing]]

OCA at 12:32, 24 May 2017

OCA — Wed, 24 May 2017 12:32:05 GMT

←Older revision		Revision as of 12:32, 24 May 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5xjl is ON HOLD	+	The entry 5xjl is ON HOLD until Paper Publication

	Authors:		Authors:

OCA: Protected "5xjl" [edit=sysop:move=sysop]

OCA — Wed, 10 May 2017 12:02:00 GMT

Protected "5xjl" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:02, 10 May 2017

OCA: New page: '''Unreleased structure''' The entry 5xjl is ON HOLD Authors: Description: Category: Unreleased Structures

OCA — Wed, 10 May 2017 12:01:59 GMT

New page: '''Unreleased structure''' The entry 5xjl is ON HOLD Authors: Description: Category: Unreleased Structures

New page

'''Unreleased structure'''

The entry 5xjl is ON HOLD

Authors:

Description:
[[Category: Unreleased Structures]]