5kxf

From Proteopedia

(Difference between revisions)

Revision as of 17:44, 19 October 2016

Crystal structure of the SPOC domain of the Arabidopsis flowering regulator FPA

Structural highlights

5kxf is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FPA_ARATH] Plays a role in the regulation of flowering time in the autonomous flowering pathway by decreasing FLOWERING LOCUS C mRNA levels. Required for RNA-mediated chromatin silencing of a range of loci in the genome. Cotranscriptionally recognizes aberrant RNA and marks it for silencing. Controls alternative cleavage and polyadenylation on pre-mRNAs and antisense RNAs. Acts redundantly with FCA to prevent the expression of distally polyadenylated antisense RNAs at the FLC locus.^[1] ^[2] ^[3]

Publication Abstract from PubMed

The Arabidopsis protein FPA controls flowering time by regulating the alternative 3'-end processing of the FLOWERING LOCUS (FLC) antisense RNA. FPA belongs to the split ends (SPEN) family of proteins, which contain N-terminal RNA recognition motifs (RRMs) and a SPEN paralog and ortholog C-terminal (SPOC) domain. The SPOC domain is highly conserved among FPA homologs in plants, but the conservation with the domain in other SPEN proteins is much lower. We have determined the crystal structure of Arabidopsis thaliana FPA SPOC domain at 2.7 A resolution. The overall structure is similar to that of the SPOC domain in human SMRT/HDAC1 Associated Repressor Protein (SHARP), although there are also substantial conformational differences between them. Structural and sequence analyses identify a surface patch that is conserved among plant FPA homologs. Mutations of two residues in this surface patch did not disrupt FPA functions, suggesting that either the SPOC domain is not required for the role of FPA in regulating RNA 3'-end formation or the functions of the FPA SPOC domain cannot be disrupted by the combination of mutations, in contrast to observations with the SHARP SPOC domain.

Crystal Structure of the SPOC Domain of the Arabidopsis Flowering Regulator FPA.,Zhang Y, Rataj K, Simpson GG, Tong L PLoS One. 2016 Aug 11;11(8):e0160694. doi: 10.1371/journal.pone.0160694., eCollection 2016. PMID:27513867^[4]

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

References

↑ Schomburg FM, Patton DA, Meinke DW, Amasino RM. FPA, a gene involved in floral induction in Arabidopsis, encodes a protein containing RNA-recognition motifs. Plant Cell. 2001 Jun;13(6):1427-36. PMID:11402170
↑ Baurle I, Smith L, Baulcombe DC, Dean C. Widespread role for the flowering-time regulators FCA and FPA in RNA-mediated chromatin silencing. Science. 2007 Oct 5;318(5847):109-12. PMID:17916737 doi:http://dx.doi.org/10.1126/science.1146565
↑ Hornyik C, Terzi LC, Simpson GG. The Spen Family Protein FPA Controls Alternative Cleavage and Polyadenylation of RNA. Dev Cell. 2010 Jan 13. PMID:20079695 doi:http://dx.doi.org/S1534-5807(09)00526-7
↑ Zhang Y, Rataj K, Simpson GG, Tong L. Crystal Structure of the SPOC Domain of the Arabidopsis Flowering Regulator FPA. PLoS One. 2016 Aug 11;11(8):e0160694. doi: 10.1371/journal.pone.0160694., eCollection 2016. PMID:27513867 doi:http://dx.doi.org/10.1371/journal.pone.0160694

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/5kxf"

Categories: Tong, L | Zhang, Y | Rna binding protein | Spoc domain arabidopsis flowering regulator

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5kxf is ON HOLD  until Paper Publication
+==Crystal structure of the SPOC domain of the Arabidopsis flowering regulator FPA==
+<StructureSection load='5kxf' size='340' side='right' caption='[[5kxf]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5kxf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KXF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KXF FirstGlance]. <br>
+</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5kxf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kxf OCA], [http://pdbe.org/5kxf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kxf RCSB], [http://www.ebi.ac.uk/pdbsum/5kxf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kxf ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/FPA_ARATH FPA_ARATH]] Plays a role in the regulation of flowering time in the autonomous flowering pathway by decreasing FLOWERING LOCUS C mRNA levels. Required for RNA-mediated chromatin silencing of a range of loci in the genome. Cotranscriptionally recognizes aberrant RNA and marks it for silencing. Controls alternative cleavage and polyadenylation on pre-mRNAs and antisense RNAs. Acts redundantly with FCA to prevent the expression of distally polyadenylated antisense RNAs at the FLC locus.<ref>PMID:11402170</ref> <ref>PMID:17916737</ref> <ref>PMID:20079695</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The Arabidopsis protein FPA controls flowering time by regulating the alternative 3'-end processing of the FLOWERING LOCUS (FLC) antisense RNA. FPA belongs to the split ends (SPEN) family of proteins, which contain N-terminal RNA recognition motifs (RRMs) and a SPEN paralog and ortholog C-terminal (SPOC) domain. The SPOC domain is highly conserved among FPA homologs in plants, but the conservation with the domain in other SPEN proteins is much lower. We have determined the crystal structure of Arabidopsis thaliana FPA SPOC domain at 2.7 A resolution. The overall structure is similar to that of the SPOC domain in human SMRT/HDAC1 Associated Repressor Protein (SHARP), although there are also substantial conformational differences between them. Structural and sequence analyses identify a surface patch that is conserved among plant FPA homologs. Mutations of two residues in this surface patch did not disrupt FPA functions, suggesting that either the SPOC domain is not required for the role of FPA in regulating RNA 3'-end formation or the functions of the FPA SPOC domain cannot be disrupted by the combination of mutations, in contrast to observations with the SHARP SPOC domain.
-Authors:
+Crystal Structure of the SPOC Domain of the Arabidopsis Flowering Regulator FPA.,Zhang Y, Rataj K, Simpson GG, Tong L PLoS One. 2016 Aug 11;11(8):e0160694. doi: 10.1371/journal.pone.0160694., eCollection 2016. PMID:27513867<ref>PMID:27513867</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5kxf" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Tong, L]]
+[[Category: Zhang, Y]]
+[[Category: Rna binding protein]]
+[[Category: Spoc domain arabidopsis flowering regulator]]

5kxf

From Proteopedia

Revision as of 17:44, 19 October 2016

Crystal structure of the SPOC domain of the Arabidopsis flowering regulator FPA

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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