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.


6dnh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:35, 13 March 2024) (edit) (undo)
 
Line 3: Line 3:
<SX load='6dnh' size='340' side='right' viewer='molstar' caption='[[6dnh]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<SX load='6dnh' size='340' side='right' viewer='molstar' caption='[[6dnh]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6dnh]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6bll 6bll]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DNH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6DNH FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6dnh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Macaca_mulatta_polyomavirus_1 Macaca mulatta polyomavirus 1]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6bll 6bll]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DNH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DNH FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CPSF1, CPSF160 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), WDR33, WDC146 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CPSF4, CPSF30, NAR, NEB1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6dnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dnh OCA], [http://pdbe.org/6dnh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dnh RCSB], [http://www.ebi.ac.uk/pdbsum/6dnh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dnh 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=6dnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dnh OCA], [https://pdbe.org/6dnh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dnh RCSB], [https://www.ebi.ac.uk/pdbsum/6dnh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dnh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/CPSF1_HUMAN CPSF1_HUMAN]] Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. This subunit is involved in the RNA recognition step of the polyadenylation reaction.<ref>PMID:14749727</ref> [[http://www.uniprot.org/uniprot/CPSF4_HUMAN CPSF4_HUMAN]] Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. CPSF4 binds RNA polymers with a preference for poly(U).<ref>PMID:9224719</ref> <ref>PMID:14749727</ref> [[http://www.uniprot.org/uniprot/WDR33_HUMAN WDR33_HUMAN]] Essential for both cleavage and polyadenylation of pre-mRNA 3' ends.<ref>PMID:19217410</ref>
+
[https://www.uniprot.org/uniprot/CPSF1_HUMAN CPSF1_HUMAN] Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. This subunit is involved in the RNA recognition step of the polyadenylation reaction.<ref>PMID:14749727</ref>
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
Nearly all eukaryotic messenger RNA precursors must undergo cleavage and polyadenylation at their 3'-end for maturation. A crucial step in this process is the recognition of the AAUAAA polyadenylation signal (PAS), and the molecular mechanism of this recognition has been a long-standing problem. Here, we report the cryo-electron microscopy structure of a quaternary complex of human CPSF-160, WDR33, CPSF-30, and an AAUAAA RNA at 3.4-A resolution. Strikingly, the AAUAAA PAS assumes an unusual conformation that allows this short motif to be bound directly by both CPSF-30 and WDR33. The A1 and A2 bases are recognized specifically by zinc finger 2 (ZF2) of CPSF-30 and the A4 and A5 bases by ZF3. Interestingly, the U3 and A6 bases form an intramolecular Hoogsteen base pair and directly contact WDR33. CPSF-160 functions as an essential scaffold and preorganizes CPSF-30 and WDR33 for high-affinity binding to AAUAAA. Our findings provide an elegant molecular explanation for how PAS sequences are recognized for mRNA 3'-end formation.
+
-
 
+
-
Molecular basis for the recognition of the human AAUAAA polyadenylation signal.,Sun Y, Zhang Y, Hamilton K, Manley JL, Shi Y, Walz T, Tong L Proc Natl Acad Sci U S A. 2017 Dec 5. pii: 1718723115. doi:, 10.1073/pnas.1718723115. PMID:29208711<ref>PMID:29208711</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 6dnh" style="background-color:#fffaf0;"></div>
+
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</SX>
</SX>
-
[[Category: Human]]
+
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Hamilton, K]]
+
[[Category: Macaca mulatta polyomavirus 1]]
-
[[Category: Sun, Y]]
+
[[Category: Hamilton K]]
-
[[Category: Tong, L]]
+
[[Category: Sun Y]]
-
[[Category: Walz, T]]
+
[[Category: Tong L]]
-
[[Category: Zhang, Y]]
+
[[Category: Walz T]]
-
[[Category: Hoogsteen base pair]]
+
[[Category: Zhang Y]]
-
[[Category: Rna binding protein-rna complex]]
+
-
[[Category: Zinc finger]]
+

Current revision

Cryo-EM structure of human CPSF-160-WDR33-CPSF-30-PAS RNA complex at 3.4 A resolution

6dnh, resolution 3.40Å

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6dnh"
Personal tools