5tee

From Proteopedia

(Difference between revisions)

Revision as of 10:02, 21 December 2022

Crystal structure of Gemin5 WD40 repeats in apo form

Structural highlights

5tee is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GEMI5_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. GEMIN5 acts as the snRNA-binding protein of the SMN complex.^[1] ^[2] ^[3]

Publication Abstract from PubMed

In cytoplasm, the survival of motor neuron (SMN) complex delivers pre-small nuclear RNAs (pre-snRNAs) to the heptameric Sm ring for the assembly of the ring complex on pre-snRNAs at the conserved Sm site [A(U)4-6G]. Gemin5, a WD40 protein component of the SMN complex, is responsible for recognizing pre-snRNAs. In addition, Gemin5 has been reported to specifically bind to the m7G cap. In this study, we show that the WD40 domain of Gemin5 is both necessary and sufficient for binding the Sm site of pre-snRNAs by isothermal titration calorimetry (ITC) and mutagenesis assays. We further determined the crystal structures of the WD40 domain of Gemin5 in complex with the Sm site or m7G cap of pre-snRNA, which reveal that the WD40 domain of Gemin5 recognizes the Sm site and m7G cap of pre-snRNAs via two distinct binding sites by respective base-specific interactions. In addition, we also uncovered a novel role of Gemin5 in escorting the truncated forms of U1 pre-snRNAs for proper disposal. Overall, the elucidated Gemin5 structures will contribute to a better understanding of Gemin5 in small nuclear ribonucleic protein (snRNP) biogenesis as well as, potentially, other cellular activities.

Structural insights into Gemin5-guided selection of pre-snRNAs for snRNP assembly.,Xu C, Ishikawa H, Izumikawa K, Li L, He H, Nobe Y, Yamauchi Y, Shahjee HM, Wu XH, Yu YT, Isobe T, Takahashi N, Min J Genes Dev. 2016 Nov 1;30(21):2376-2390. Epub 2016 Nov 10. PMID:27881600^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gubitz AK, Mourelatos Z, Abel L, Rappsilber J, Mann M, Dreyfuss G. Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins. J Biol Chem. 2002 Feb 15;277(7):5631-6. Epub 2001 Nov 19. PMID:11714716 doi:http://dx.doi.org/10.1074/jbc.M109448200
↑ Battle DJ, Lau CK, Wan L, Deng H, Lotti F, Dreyfuss G. The Gemin5 protein of the SMN complex identifies snRNAs. Mol Cell. 2006 Jul 21;23(2):273-9. PMID:16857593 doi:http://dx.doi.org/S1097-2765(06)00378-9
↑ Chari A, Golas MM, Klingenhager M, Neuenkirchen N, Sander B, Englbrecht C, Sickmann A, Stark H, Fischer U. An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs. Cell. 2008 Oct 31;135(3):497-509. doi: 10.1016/j.cell.2008.09.020. PMID:18984161 doi:http://dx.doi.org/10.1016/j.cell.2008.09.020
↑ Xu C, Ishikawa H, Izumikawa K, Li L, He H, Nobe Y, Yamauchi Y, Shahjee HM, Wu XH, Yu YT, Isobe T, Takahashi N, Min J. Structural insights into Gemin5-guided selection of pre-snRNAs for snRNP assembly. Genes Dev. 2016 Nov 1;30(21):2376-2390. Epub 2016 Nov 10. PMID:27881600 doi:http://dx.doi.org/10.1101/gad.288340.116

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5tee"

@@ Line 3: / Line 3: @@
 <StructureSection load='5tee' size='340' side='right'caption='[[5tee]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5tee]] 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=5TEE OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5TEE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5tee]] 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=5TEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TEE FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tef|5tef]]</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=5tee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tee OCA], [https://pdbe.org/5tee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tee RCSB], [https://www.ebi.ac.uk/pdbsum/5tee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tee ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GEMIN5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5tee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tee OCA], [http://pdbe.org/5tee PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tee RCSB], [http://www.ebi.ac.uk/pdbsum/5tee PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tee ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GEMI5_HUMAN GEMI5_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. GEMIN5 acts as the snRNA-binding protein of the SMN complex.<ref>PMID:11714716</ref> <ref>PMID:16857593</ref> <ref>PMID:18984161</ref>
+[https://www.uniprot.org/uniprot/GEMI5_HUMAN GEMI5_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. GEMIN5 acts as the snRNA-binding protein of the SMN complex.<ref>PMID:11714716</ref> <ref>PMID:16857593</ref> <ref>PMID:18984161</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Arrowsmith, C H]]
+[[Category: Arrowsmith CH]]
-[[Category: Bian, C]]
+[[Category: Bian C]]
-[[Category: Bountra, C]]
+[[Category: Bountra C]]
-[[Category: Cerovina, T]]
+[[Category: Cerovina T]]
-[[Category: Chao, X]]
+[[Category: Chao X]]
-[[Category: Edwards, A M]]
+[[Category: Edwards AM]]
-[[Category: He, H]]
+[[Category: He H]]
-[[Category: Min, J]]
+[[Category: Min J]]
-[[Category: Structural genomic]]
+[[Category: Seitova A]]
-[[Category: Seitova, A]]
+[[Category: Tempel W]]
-[[Category: Tempel, W]]
+[[Category: Walker JR]]
-[[Category: Walker, J R]]
-[[Category: Sgc]]
-[[Category: Splicing]]

5tee

From Proteopedia

Revision as of 10:02, 21 December 2022

Crystal structure of Gemin5 WD40 repeats in apo form

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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