3nwt

From Proteopedia

(Difference between revisions)

Revision as of 07:11, 12 May 2022

Crystal structure of the N-terminal domain of the yeast telomere-binding and telomerase regulatory protein Cdc13

Structural highlights

3nwt is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3nws
Gene:	CDC13, YDL220C (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CDC13_YEAST] Single-stranded telomeric DNA-binding protein that regulates telomere replication. Has a role in both positive and negative regulation. Promotes [TG(1-3)] strand lengthening via interaction with EST1. Promotes [C(1-3)A] strand re-synthesis by DNA polymerase alpha via interaction with POL1. Negatively regulates telomere elongation of the G strand via binding with STN1 thereby inhibiting telomerase activity.^[1] ^[2] ^[3]

Publication Abstract from PubMed

The essential yeast protein Cdc13 facilitates chromosome end replication by recruiting telomerase to telomeres, and together with its interacting partners Stn1 and Ten1, it protects chromosome ends from nucleolytic attack, thus contributing to genome integrity. Although Cdc13 has been studied extensively, the precise role of its N-terminal domain (Cdc13N) in telomere length regulation remains unclear. Here we present a structural, biochemical, and functional characterization of Cdc13N. The structure reveals that this domain comprises an oligonucleotide/oligosaccharide binding (OB) fold and is involved in Cdc13 dimerization. Biochemical data show that Cdc13N weakly binds long, single-stranded, telomeric DNA in a fashion that is directly dependent on domain oligomerization. When introduced into full-length Cdc13 in vivo, point mutations that prevented Cdc13N dimerization or DNA binding caused telomere shortening or lengthening, respectively. The multiple DNA binding domains and dimeric nature of Cdc13 offer unique insights into how it coordinates the recruitment and regulation of telomerase access to the telomeres.

Cdc13 N-terminal dimerization, DNA binding, and telomere length regulation.,Mitchell MT, Smith JS, Mason M, Harper S, Speicher DW, Johnson FB, Skordalakes E Mol Cell Biol. 2010 Nov;30(22):5325-34. Epub 2010 Sep 13. PMID:20837709^[4]

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

References

↑ Chandra A, Hughes TR, Nugent CI, Lundblad V. Cdc13 both positively and negatively regulates telomere replication. Genes Dev. 2001 Feb 15;15(4):404-14. PMID:11230149 doi:10.1101/gad.861001
↑ Meier B, Driller L, Jaklin S, Feldmann HM. New function of CDC13 in positive telomere length regulation. Mol Cell Biol. 2001 Jul;21(13):4233-45. PMID:11390652 doi:10.1128/MCB.21.13.4233-4245.2001
↑ Qi H, Zakian VA. The Saccharomyces telomere-binding protein Cdc13p interacts with both the catalytic subunit of DNA polymerase alpha and the telomerase-associated est1 protein. Genes Dev. 2000 Jul 15;14(14):1777-88. PMID:10898792
↑ Mitchell MT, Smith JS, Mason M, Harper S, Speicher DW, Johnson FB, Skordalakes E. Cdc13 N-terminal dimerization, DNA binding, and telomere length regulation. Mol Cell Biol. 2010 Nov;30(22):5325-34. Epub 2010 Sep 13. PMID:20837709 doi:10.1128/MCB.00515-10

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/3nwt"

@@ Line 3: / Line 3: @@
 <StructureSection load='3nwt' size='340' side='right'caption='[[3nwt]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3nwt]] is a 1 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=3NWT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NWT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3nwt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NWT FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nws|3nws]]</td></tr>
+</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3nws|3nws]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDC13, YDL220C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDC13, YDL220C ([https://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=3nwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nwt OCA], [http://pdbe.org/3nwt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nwt RCSB], [http://www.ebi.ac.uk/pdbsum/3nwt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nwt 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=3nwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nwt OCA], [https://pdbe.org/3nwt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nwt RCSB], [https://www.ebi.ac.uk/pdbsum/3nwt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nwt ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CDC13_YEAST CDC13_YEAST]] Single-stranded telomeric DNA-binding protein that regulates telomere replication. Has a role in both positive and negative regulation. Promotes [TG(1-3)] strand lengthening via interaction with EST1. Promotes [C(1-3)A] strand re-synthesis by DNA polymerase alpha via interaction with POL1. Negatively regulates telomere elongation of the G strand via binding with STN1 thereby inhibiting telomerase activity.<ref>PMID:11230149</ref> <ref>PMID:11390652</ref> <ref>PMID:10898792</ref>
+[[https://www.uniprot.org/uniprot/CDC13_YEAST CDC13_YEAST]] Single-stranded telomeric DNA-binding protein that regulates telomere replication. Has a role in both positive and negative regulation. Promotes [TG(1-3)] strand lengthening via interaction with EST1. Promotes [C(1-3)A] strand re-synthesis by DNA polymerase alpha via interaction with POL1. Negatively regulates telomere elongation of the G strand via binding with STN1 thereby inhibiting telomerase activity.<ref>PMID:11230149</ref> <ref>PMID:11390652</ref> <ref>PMID:10898792</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

3nwt

From Proteopedia

Revision as of 07:11, 12 May 2022

Crystal structure of the N-terminal domain of the yeast telomere-binding and telomerase regulatory protein Cdc13

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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