This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2osq

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:14, 22 August 2018

NMR Structure of RRM-1 of Yeast NPL3 Protein

Structural highlights

2osq is a 1 chain structure with sequence from Atcc 18824. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2osr
Gene:	NOP3, MTS1, NAB1, NPL3 (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NOP3_YEAST] Required for pre-rRNA processing and nuclear import as well as mitochondrial protein targeting. Binds to poly(A).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Yeast Npl3 is homologous to SR proteins in higher eukaryotes, a family of RNA-binding proteins that have multiple essential roles in RNA metabolism. This protein competes with 3'-end processing factors for binding to the nascent RNA, protecting the transcript from premature termination and coordinating transcription termination and the packaging of the fully processed transcript for export. The NMR structure of its RNA-binding domain shows two unusually compact RNA recognition motifs (RRMs), and identifies the RNA recognition surface in Npl3. Biochemical and NMR studies identify a class of G+U-rich RNA sequences with high specificity for this protein. The protein binds to RNA and forms a single globular structure, but the two RRMs of Npl3 are not equivalent, with the second domain forming much stronger interactions with G+U-rich RNA sequences that occur independently of the interaction of the first RRM. The specific binding to G+U-rich RNAs observed for the two RRMs of Npl3 is masked in the full-length protein by a much stronger but non-sequence-specific RNA-binding activity residing outside of its RRMs. The preference of Npl3 for G+U-rich sequences supports the model for its function in regulating recognition of 3'-end processing sites through competition with the Rna15 (yeast analog of human CstF-64 protein) subunit of the processing complex.

Structure of the yeast SR protein Npl3 and Interaction with mRNA 3'-end processing signals.,Deka P, Bucheli ME, Moore C, Buratowski S, Varani G J Mol Biol. 2008 Jan 4;375(1):136-50. Epub 2007 Sep 16. PMID:18022637^[1]

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

References

↑ Deka P, Bucheli ME, Moore C, Buratowski S, Varani G. Structure of the yeast SR protein Npl3 and Interaction with mRNA 3'-end processing signals. J Mol Biol. 2008 Jan 4;375(1):136-50. Epub 2007 Sep 16. PMID:18022637 doi:10.1016/j.jmb.2007.09.029

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2osq"

@@ Line 1: / Line 1: @@
 ==NMR Structure of RRM-1 of Yeast NPL3 Protein==
 <StructureSection load='2osq' size='340' side='right' caption='[[2osq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2osr|2osr]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NOP3, MTS1, NAB1, NPL3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=2osq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2osq OCA], [http://pdbe.org/2osq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2osq RCSB], [http://www.ebi.ac.uk/pdbsum/2osq 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=2osq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2osq OCA], [http://pdbe.org/2osq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2osq RCSB], [http://www.ebi.ac.uk/pdbsum/2osq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2osq ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/os/2osq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/os/2osq_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

2osq

From Proteopedia

Revision as of 07:14, 22 August 2018

NMR Structure of RRM-1 of Yeast NPL3 Protein

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox