4f92 - Revision history

OCA at 11:11, 1 March 2024

2024-03-01T11:11:47Z

←Older revision		Revision as of 11:11, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4f92]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F92 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4f92]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F92 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAN:SULFANILAMIDE'>SAN</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]] 2.662Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAN:SULFANILAMIDE'>SAN</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=4f92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f92 OCA], [https://pdbe.org/4f92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f92 RCSB], [https://www.ebi.ac.uk/pdbsum/4f92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f92 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=4f92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f92 OCA], [https://pdbe.org/4f92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f92 RCSB], [https://www.ebi.ac.uk/pdbsum/4f92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f92 ProSAT]</span></td></tr>
	</table>		</table>
Line 11:		Line 12:
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/U520_HUMAN U520_HUMAN] RNA helicase that plays an essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes. Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome.<ref>PMID:16723661</ref> <ref>PMID:8670905</ref> <ref>PMID:9539711</ref> <ref>PMID:23045696</ref>		[https://www.uniprot.org/uniprot/U520_HUMAN U520_HUMAN] RNA helicase that plays an essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes. Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome.<ref>PMID:16723661</ref> <ref>PMID:8670905</ref> <ref>PMID:9539711</ref> <ref>PMID:23045696</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Assembly of a spliceosome, catalyzing precursor-messenger RNA splicing, involves multiple RNA-protein remodeling steps, driven by eight conserved DEXD/H-box RNA helicases. The 250-kDa Brr2 enzyme, which is essential for U4/U6 di-small nuclear ribonucleoprotein disruption during spliceosome catalytic activation and for spliceosome disassembly, is the only member of this group that is permanently associated with the spliceosome, thus requiring its faithful regulation. At the same time, Brr2 represents a unique subclass of superfamily 2 nucleic acid helicases, containing tandem helicase cassettes. Presently, the mechanistic and regulatory consequences of this unconventional architecture are unknown. Here we show that in human Brr2, two ring-like helicase cassettes intimately interact and functionally cooperate and how retinitis pigmentosa-linked Brr2 mutations interfere with the enzyme's function. Only the N-terminal cassette harbors ATPase and helicase activities in isolation. Comparison with other helicases and mutational analyses show how it threads single-stranded RNA, and structural features suggest how it can load onto an internal region of U4/U6 di-snRNA. Although the C-terminal cassette does not seem to engage RNA in the same fashion, it binds ATP and strongly stimulates the N-terminal helicase. Mutations at the cassette interface, in an intercassette linker or in the C-terminal ATP pocket, affect this cross-talk in diverse ways. Together, our results reveal the structural and functional interplay between two helicase cassettes in a tandem superfamily 2 enzyme and point to several sites through which Brr2 activity may be regulated.

-	Structural basis for functional cooperation between tandem helicase cassettes in Brr2-mediated remodeling of the spliceosome.,Santos KF, Jovin SM, Weber G, Pena V, Luhrmann R, Wahl MC Proc Natl Acad Sci U S A. 2012 Oct 8. PMID:23045696<ref>PMID:23045696</ref>	+	==See Also==
-		+	*[[Helicase 3D structures\|Helicase 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class~~=~~"pdbe-citations 4f92" style~~=~~"background-color:#fffaf0;"></div>~~	+
	== References ==		== References ==
	<references/>		<references/>

OCA at 04:42, 7 October 2022

2022-10-07T04:42:14Z

←Older revision		Revision as of 04:42, 7 October 2022
Line 1:		Line 1:

	==Brr2 Helicase Region S1087L==		==Brr2 Helicase Region S1087L==
-	<StructureSection load='4f92' size='340' side='right' caption='[[4f92]], [[Resolution\|resolution]] 2.66Å' scene=''>	+	<StructureSection load='4f92' size='340' side='right'caption='[[4f92]], [[Resolution\|resolution]] 2.66Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4f92]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F92 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4F92 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4f92]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F92 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAN:SULFANILAMIDE'>SAN</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAN:SULFANILAMIDE'>SAN</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4f91\|4f91]], [[4f93\|4f93]]</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=4f92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f92 OCA], [https://pdbe.org/4f92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f92 RCSB], [https://www.ebi.ac.uk/pdbsum/4f92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f92 ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SNRNP200, ASCC3L1, HELIC2, KIAA0788 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA_helicase RNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.13 3.6.4.13] </span></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=4f92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f92 OCA], [~~http~~://pdbe.org/4f92 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4f92 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4f92 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4f92 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/U520_HUMAN U520_HUMAN]] Retinitis pigmentosa. Retinitis pigmentosa 33 (RP33) [MIM:[~~http~~://omim.org/entry/610359 610359]]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:16723661</ref> <ref>PMID:23045696</ref> <ref>PMID:19878916</ref> <ref>PMID:19710410</ref> <ref>PMID:21618346</ref>	+	[https://www.uniprot.org/uniprot/U520_HUMAN U520_HUMAN] Retinitis pigmentosa. Retinitis pigmentosa 33 (RP33) [MIM:[https://omim.org/entry/610359 610359]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:16723661</ref> <ref>PMID:23045696</ref> <ref>PMID:19878916</ref> <ref>PMID:19710410</ref> <ref>PMID:21618346</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/U520_HUMAN U520_HUMAN]] RNA helicase that plays an essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes. Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome.<ref>PMID:16723661</ref> <ref>PMID:8670905</ref> <ref>PMID:9539711</ref> <ref>PMID:23045696</ref>	+	[https://www.uniprot.org/uniprot/U520_HUMAN U520_HUMAN] RNA helicase that plays an essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes. Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome.<ref>PMID:16723661</ref> <ref>PMID:8670905</ref> <ref>PMID:9539711</ref> <ref>PMID:23045696</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 27:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~RNA helicase~~]]	+	[[Category: Large Structures]]
-	[[Category: Jovin~~, S M~~]]	+	[[Category: Jovin SM]]
-	[[Category: Luehrmann, R]]	+	[[Category: Luehrmann R]]
-	[[Category: Pena, V]]	+	[[Category: Pena V]]
-	[[Category: Santos~~, K F~~]]	+	[[Category: Santos KF]]
-	[[Category: Wahl~~, M C~~]]	+	[[Category: Wahl MC]]
-	[[Category: Weber, G]]	+	[[Category: Weber G]]
-	~~[[Category: Dexd/h-box rna helicase]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Nucleus]]~~	+
-	~~[[Category: Pre-mrna splicing]]~~	+
-	~~[[Category: Rna and atp binding]]~~	+
-	~~[[Category: Rnp remodeling]]~~	+
-	~~[[Category: Spliceosome catalytic activation~~]]	+

OCA at 19:48, 15 December 2016

2016-12-15T19:48:21Z

←Older revision		Revision as of 19:48, 15 December 2016
Line 1:		Line 1:
		+
	==Brr2 Helicase Region S1087L==		==Brr2 Helicase Region S1087L==
	<StructureSection load='4f92' size='340' side='right' caption='[[4f92]], [[Resolution\|resolution]] 2.66Å' scene=''>		<StructureSection load='4f92' size='340' side='right' caption='[[4f92]], [[Resolution\|resolution]] 2.66Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4f92]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F92 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F92 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4f92]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F92 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F92 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAN:SULFANILAMIDE'>SAN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAN:SULFANILAMIDE'>SAN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4f91\|4f91]], [[4f93\|4f93]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4f91\|4f91]], [[4f93\|4f93]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SNRNP200, ASCC3L1, HELIC2, KIAA0788 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SNRNP200, ASCC3L1, HELIC2, KIAA0788 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA_helicase RNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.13 3.6.4.13] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA_helicase RNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.13 3.6.4.13] </span></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=4f92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f92 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f92 RCSB], [http://www.ebi.ac.uk/pdbsum/4f92 PDBsum]</span></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=4f92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f92 OCA], [http://pdbe.org/4f92 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4f92 RCSB], [http://www.ebi.ac.uk/pdbsum/4f92 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4f92 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 21:		Line 22:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4f92" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: RNA helicase]]		[[Category: RNA helicase]]
	[[Category: Jovin, S M]]		[[Category: Jovin, S M]]

OCA at 14:17, 9 December 2014

2014-12-09T14:17:42Z

←Older revision		Revision as of 14:17, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~4f92.~~png~~\|~~left~~\|~~200px~~]]	+	==Brr2 Helicase Region S1087L==
		+	<StructureSection load='4f92' size='340' side='right' caption='[[4f92]], [[Resolution\|resolution]] 2.66Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4f92]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F92 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F92 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAN:SULFANILAMIDE'>SAN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4f91\|4f91]], [[4f93\|4f93]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SNRNP200, ASCC3L1, HELIC2, KIAA0788 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA_helicase RNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.13 3.6.4.13] </span></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=4f92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f92 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f92 RCSB], [http://www.ebi.ac.uk/pdbsum/4f92 PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/U520_HUMAN U520_HUMAN]] Retinitis pigmentosa. Retinitis pigmentosa 33 (RP33) [MIM:[http://omim.org/entry/610359 610359]]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Note=The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:16723661</ref> <ref>PMID:23045696</ref> <ref>PMID:19878916</ref> <ref>PMID:19710410</ref> <ref>PMID:21618346</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/U520_HUMAN U520_HUMAN]] RNA helicase that plays an essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes. Involved in spliceosome assembly, activation and disassembly. Mediates changes in the dynamic network of RNA-RNA interactions in the spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA duplices, an essential step in the assembly of a catalytically active spliceosome.<ref>PMID:16723661</ref> <ref>PMID:8670905</ref> <ref>PMID:9539711</ref> <ref>PMID:23045696</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Assembly of a spliceosome, catalyzing precursor-messenger RNA splicing, involves multiple RNA-protein remodeling steps, driven by eight conserved DEXD/H-box RNA helicases. The 250-kDa Brr2 enzyme, which is essential for U4/U6 di-small nuclear ribonucleoprotein disruption during spliceosome catalytic activation and for spliceosome disassembly, is the only member of this group that is permanently associated with the spliceosome, thus requiring its faithful regulation. At the same time, Brr2 represents a unique subclass of superfamily 2 nucleic acid helicases, containing tandem helicase cassettes. Presently, the mechanistic and regulatory consequences of this unconventional architecture are unknown. Here we show that in human Brr2, two ring-like helicase cassettes intimately interact and functionally cooperate and how retinitis pigmentosa-linked Brr2 mutations interfere with the enzyme's function. Only the N-terminal cassette harbors ATPase and helicase activities in isolation. Comparison with other helicases and mutational analyses show how it threads single-stranded RNA, and structural features suggest how it can load onto an internal region of U4/U6 di-snRNA. Although the C-terminal cassette does not seem to engage RNA in the same fashion, it binds ATP and strongly stimulates the N-terminal helicase. Mutations at the cassette interface, in an intercassette linker or in the C-terminal ATP pocket, affect this cross-talk in diverse ways. Together, our results reveal the structural and functional interplay between two helicase cassettes in a tandem superfamily 2 enzyme and point to several sites through which Brr2 activity may be regulated.

-	~~{{STRUCTURE_4f92\| PDB=4f92 \| SCENE= }}~~	+	Structural basis for functional cooperation between tandem helicase cassettes in Brr2-mediated remodeling of the spliceosome.,Santos KF, Jovin SM, Weber G, Pena V, Luhrmann R, Wahl MC Proc Natl Acad Sci U S A. 2012 Oct 8. PMID:23045696<ref>PMID:23045696</ref>

-	~~===Brr2 Helicase Region S1087L===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_23045696}}~~	+	== References ==
-		+	<references/>
-	==~~About this Structure~~==	+	__TOC__
-	~~[[4f92]] is a 1 chain structure with sequence from [http:~~//~~en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F92 OCA].~~	+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: RNA helicase]]		[[Category: RNA helicase]]
-	[[Category: Jovin, S M.]]	+	[[Category: Jovin, S M]]
-	[[Category: Luehrmann, R.]]	+	[[Category: Luehrmann, R]]
-	[[Category: Pena, V.]]	+	[[Category: Pena, V]]
-	[[Category: Santos, K F.]]	+	[[Category: Santos, K F]]
-	[[Category: Wahl, M C.]]	+	[[Category: Wahl, M C]]
-	[[Category: Weber, G.]]	+	[[Category: Weber, G]]
	[[Category: Dexd/h-box rna helicase]]		[[Category: Dexd/h-box rna helicase]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 14:54, 28 November 2012

2012-11-28T14:54:35Z

←Older revision		Revision as of 14:54, 28 November 2012
Line 5:		Line 5:
	===Brr2 Helicase Region S1087L===		===Brr2 Helicase Region S1087L===

		+	{{ABSTRACT_PUBMED_23045696}}

	==About this Structure==		==About this Structure==

OCA at 14:14, 8 November 2012

2012-11-08T14:14:48Z

←Older revision		Revision as of 14:14, 8 November 2012
Line 5:		Line 5:
	===Brr2 Helicase Region S1087L===		===Brr2 Helicase Region S1087L===

-	{{ABSTRACT_PUBMED_23045696}}

	==About this Structure==		==About this Structure==

OCA at 06:19, 24 October 2012

2012-10-24T06:19:05Z

←Older revision		Revision as of 06:19, 24 October 2012
Line 1:		Line 1:
-	[[Image:4f92.~~jpg~~\|left\|200px]]	+	[[Image:4f92.png\|left\|200px]]

	{{STRUCTURE_4f92\| PDB=4f92 \| SCENE= }}		{{STRUCTURE_4f92\| PDB=4f92 \| SCENE= }}
Line 5:		Line 5:
	===Brr2 Helicase Region S1087L===		===Brr2 Helicase Region S1087L===

		+	{{ABSTRACT_PUBMED_23045696}}

	==About this Structure==		==About this Structure==

OCA at 07:11, 17 October 2012

2012-10-17T07:11:53Z

←Older revision		Revision as of 07:11, 17 October 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:4f92.jpg\|left\|200px]]

-	~~The entry~~ 4f92 ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_4f92\| PDB=4f92 \| SCENE= }}

-	~~Authors: Santos, K.F., Jovin, S.M., Weber, G., Pena, V., Luehrmann, R., Wahl, M.C.~~	+	===Brr2 Helicase Region S1087L===

-	~~Description~~: ~~Brr2 Helicase Region S1087L~~	+
		+	==About this Structure==
		+	[[4f92]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F92 OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: RNA helicase]]
		+	[[Category: Jovin, S M.]]
		+	[[Category: Luehrmann, R.]]
		+	[[Category: Pena, V.]]
		+	[[Category: Santos, K F.]]
		+	[[Category: Wahl, M C.]]
		+	[[Category: Weber, G.]]
		+	[[Category: Dexd/h-box rna helicase]]
		+	[[Category: Hydrolase]]
		+	[[Category: Nucleus]]
		+	[[Category: Pre-mrna splicing]]
		+	[[Category: Rna and atp binding]]
		+	[[Category: Rnp remodeling]]
		+	[[Category: Spliceosome catalytic activation]]

OCA at 07:15, 4 July 2012

2012-07-04T07:15:05Z

←Older revision		Revision as of 07:15, 4 July 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4f92 is ON HOLD	+	The entry 4f92 is ON HOLD until Paper Publication

	Authors: Santos, K.F., Jovin, S.M., Weber, G., Pena, V., Luehrmann, R., Wahl, M.C.		Authors: Santos, K.F., Jovin, S.M., Weber, G., Pena, V., Luehrmann, R., Wahl, M.C.

	Description: Brr2 Helicase Region S1087L		Description: Brr2 Helicase Region S1087L

OCA: Protected "4f92" [edit=sysop:move=sysop]

2012-05-30T05:32:29Z

Protected "4f92" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:32, 30 May 2012