8eqb

From Proteopedia

(Difference between revisions)

Current revision

FAM46C/BCCIPalpha/Nanobody complex

Structural highlights

8eqb is a 12 chain structure with sequence from Homo sapiens and Lama glama. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 6.5Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TET5C_HUMAN Nucleotidyltransferase that act as a non-canonical poly(A) RNA polymerase which enhances mRNA stability and gene expression. Mainly targets mRNAs encoding endoplasmic reticulum-targeted protein and may be involved in induction of cell death.^[1] ^[2] (Microbial infection) Seems to enhance replication of some viruses, including yellow fever virus, in response to type I interferon.^[3]

Publication Abstract from PubMed

The FAM46 (also known as TENT5) proteins are noncanonical poly(A) polymerases (PAPs) implicated in regulating RNA stability. The regulatory mechanisms of FAM46 are poorly understood. Here, we report that the nuclear protein BCCIPalpha, but not the alternatively spliced isoform BCCIPbeta, binds FAM46 and inhibits their PAP activity. Unexpectedly, our structures of the FAM46A/BCCIPalpha and FAM46C/BCCIPalpha complexes show that, despite sharing most of the sequence and differing only at the C-terminal portion, BCCIPalpha adopts a unique structure completely different from BCCIPbeta. The distinct C-terminal segment of BCCIPalpha supports the adoption of the unique fold but does not directly interact with FAM46. The beta sheets in BCCIPalpha and FAM46 pack side by side to form an extended beta sheet. A helix-loop-helix segment in BCCIPalpha inserts into the active site cleft of FAM46, thereby inhibiting the PAP activity. Our results together show that the unique fold of BCCIPalpha underlies its interaction with and functional regulation of FAM46.

Inhibition of FAM46/TENT5 activity by BCCIPalpha adopting a unique fold.,Liu S, Chen H, Yin Y, Lu D, Gao G, Li J, Bai XC, Zhang X Sci Adv. 2023 Apr 5;9(14):eadf5583. doi: 10.1126/sciadv.adf5583. Epub 2023 Apr 5. PMID:37018411^[4]

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

References

↑ Kuchta K, Muszewska A, Knizewski L, Steczkiewicz K, Wyrwicz LS, Pawlowski K, Rychlewski L, Ginalski K. FAM46 proteins are novel eukaryotic non-canonical poly(A) polymerases. Nucleic Acids Res. 2016 May 5;44(8):3534-48. doi: 10.1093/nar/gkw222. Epub 2016, Apr 7. PMID:27060136 doi:http://dx.doi.org/10.1093/nar/gkw222
↑ Mroczek S, Chlebowska J, Kulinski TM, Gewartowska O, Gruchota J, Cysewski D, Liudkovska V, Borsuk E, Nowis D, Dziembowski A. The non-canonical poly(A) polymerase FAM46C acts as an onco-suppressor in multiple myeloma. Nat Commun. 2017 Sep 20;8(1):619. doi: 10.1038/s41467-017-00578-5. PMID:28931820 doi:http://dx.doi.org/10.1038/s41467-017-00578-5
↑ Schoggins JW, Wilson SJ, Panis M, Murphy MY, Jones CT, Bieniasz P, Rice CM. A diverse range of gene products are effectors of the type I interferon antiviral response. Nature. 2011 Apr 28;472(7344):481-5. doi: 10.1038/nature09907. Epub 2011 Apr 10. PMID:21478870 doi:10.1038/nature09907
↑ Liu S, Chen H, Yin Y, Lu D, Gao G, Li J, Bai XC, Zhang X. Inhibition of FAM46/TENT5 activity by BCCIPα adopting a unique fold. Sci Adv. 2023 Apr 5;9(14):eadf5583. PMID:37018411 doi:10.1126/sciadv.adf5583

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/8eqb"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 8eqb is ON HOLD  until Paper Publication
+==FAM46C/BCCIPalpha/Nanobody complex==
+<StructureSection load='8eqb' size='340' side='right'caption='[[8eqb]], [[Resolution|resolution]] 6.50&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8eqb]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EQB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EQB FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.5&#8491;</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=8eqb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8eqb OCA], [https://pdbe.org/8eqb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8eqb RCSB], [https://www.ebi.ac.uk/pdbsum/8eqb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8eqb ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TET5C_HUMAN TET5C_HUMAN] Nucleotidyltransferase that act as a non-canonical poly(A) RNA polymerase which enhances mRNA stability and gene expression. Mainly targets mRNAs encoding endoplasmic reticulum-targeted protein and may be involved in induction of cell death.<ref>PMID:27060136</ref> <ref>PMID:28931820</ref>   (Microbial infection) Seems to enhance replication of some viruses, including yellow fever virus, in response to type I interferon.<ref>PMID:21478870</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The FAM46 (also known as TENT5) proteins are noncanonical poly(A) polymerases (PAPs) implicated in regulating RNA stability. The regulatory mechanisms of FAM46 are poorly understood. Here, we report that the nuclear protein BCCIPalpha, but not the alternatively spliced isoform BCCIPbeta, binds FAM46 and inhibits their PAP activity. Unexpectedly, our structures of the FAM46A/BCCIPalpha and FAM46C/BCCIPalpha complexes show that, despite sharing most of the sequence and differing only at the C-terminal portion, BCCIPalpha adopts a unique structure completely different from BCCIPbeta. The distinct C-terminal segment of BCCIPalpha supports the adoption of the unique fold but does not directly interact with FAM46. The beta sheets in BCCIPalpha and FAM46 pack side by side to form an extended beta sheet. A helix-loop-helix segment in BCCIPalpha inserts into the active site cleft of FAM46, thereby inhibiting the PAP activity. Our results together show that the unique fold of BCCIPalpha underlies its interaction with and functional regulation of FAM46.
-Authors:
+Inhibition of FAM46/TENT5 activity by BCCIPalpha adopting a unique fold.,Liu S, Chen H, Yin Y, Lu D, Gao G, Li J, Bai XC, Zhang X Sci Adv. 2023 Apr 5;9(14):eadf5583. doi: 10.1126/sciadv.adf5583. Epub 2023 Apr 5. PMID:37018411<ref>PMID:37018411</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 8eqb" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Lama glama]]
+[[Category: Large Structures]]
+[[Category: Bai X]]
+[[Category: Chen H]]
+[[Category: Liu S]]
+[[Category: Yin Y]]
+[[Category: Zhang X]]

8eqb

From Proteopedia

Current revision

FAM46C/BCCIPalpha/Nanobody complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox