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5hog

From Proteopedia

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Current revision

Crystal structure of the carboxy-terminal domain of yeast Ctf4 bound to Dna2.

Structural highlights

5hog is a 5 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.092Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CTF4_YEAST Accessory factor for DNA replication. It plays a role in accurately duplicating the genome in vivo.

Publication Abstract from PubMed

Replisome assembly at eukaryotic replication forks connects the DNA helicase to DNA polymerases and many other factors. The helicase binds the leading-strand polymerase directly, but is connected to the Pol alpha lagging-strand polymerase by the trimeric adaptor Ctf4. Here, we identify new Ctf4 partners in addition to Pol alpha and helicase, all of which contain a "Ctf4-interacting-peptide" or CIP-box. Crystallographic analysis classifies CIP-boxes into two related groups that target different sites on Ctf4. Mutations in the CIP-box motifs of the Dna2 nuclease or the rDNA-associated protein Tof2 do not perturb DNA synthesis genome-wide, but instead lead to a dramatic shortening of chromosome 12 that contains the large array of rDNA repeats. Our data reveal unexpected complexity of Ctf4 function, as a hub that connects multiple accessory factors to the replisome. Most strikingly, Ctf4-dependent recruitment of CIP-box proteins couples other processes to DNA synthesis, including rDNA copy-number regulation.

Ctf4 Is a Hub in the Eukaryotic Replisome that Links Multiple CIP-Box Proteins to the CMG Helicase.,Villa F, Simon AC, Ortiz Bazan MA, Kilkenny ML, Wirthensohn D, Wightman M, Matak-Vinkovic D, Pellegrini L, Labib K Mol Cell. 2016 Jul 5. pii: S1097-2765(16)30240-4. doi:, 10.1016/j.molcel.2016.06.009. PMID:27397685^[1]

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

References

↑ Villa F, Simon AC, Ortiz Bazan MA, Kilkenny ML, Wirthensohn D, Wightman M, Matak-Vinkovic D, Pellegrini L, Labib K. Ctf4 Is a Hub in the Eukaryotic Replisome that Links Multiple CIP-Box Proteins to the CMG Helicase. Mol Cell. 2016 Jul 5. pii: S1097-2765(16)30240-4. doi:, 10.1016/j.molcel.2016.06.009. PMID:27397685 doi:http://dx.doi.org/10.1016/j.molcel.2016.06.009

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/5hog"

Categories: Large Structures | Saccharomyces cerevisiae | Pellegrini L | Simon AC

@@ Line 3: / Line 3: @@
 <StructureSection load='5hog' size='340' side='right'caption='[[5hog]], [[Resolution|resolution]] 3.09&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5hog]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HOG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5HOG FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5hog]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HOG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5HOG FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c8s|4c8s]], [[4c93|4c93]], [[4c95|4c95]], [[4c8h|4c8h]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.092&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTF4, CHL15, POB1, YPR135W, P9659.7 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=5hog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hog OCA], [https://pdbe.org/5hog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5hog RCSB], [https://www.ebi.ac.uk/pdbsum/5hog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5hog ProSAT]</span></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=5hog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hog OCA], [http://pdbe.org/5hog PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hog RCSB], [http://www.ebi.ac.uk/pdbsum/5hog PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hog ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CTF4_YEAST CTF4_YEAST]] Accessory factor for DNA replication. It plays a role in accurately duplicating the genome in vivo.
+[https://www.uniprot.org/uniprot/CTF4_YEAST CTF4_YEAST] Accessory factor for DNA replication. It plays a role in accurately duplicating the genome in vivo.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
 [[Category: Large Structures]]
-[[Category: Pellegrini, L]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Simon, A C]]
+[[Category: Pellegrini L]]
-[[Category: Adaptor protein]]
+[[Category: Simon AC]]
-[[Category: Beta-propeller domain]]
-[[Category: Dna replication]]
-[[Category: Replication]]

5hog

From Proteopedia

Current revision

Crystal structure of the carboxy-terminal domain of yeast Ctf4 bound to Dna2.

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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