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{{STRUCTURE_1d8b|  PDB=1d8b  |  SCENE=  }}
'''NMR STRUCTURE OF THE HRDC DOMAIN FROM SACCHAROMYCES CEREVISIAE RECQ HELICASE'''


==NMR STRUCTURE OF THE HRDC DOMAIN FROM SACCHAROMYCES CEREVISIAE RECQ HELICASE==
<StructureSection load='1d8b' size='340' side='right'caption='[[1d8b]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1d8b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D8B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D8B FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1d8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d8b OCA], [https://pdbe.org/1d8b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d8b RCSB], [https://www.ebi.ac.uk/pdbsum/1d8b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d8b ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SGS1_YEAST SGS1_YEAST] Interacts with topoisomerases II and TOP3. Could create a deleterious topological substrate that TOP3 preferentially resolves. The TOP3-SGS1 protein complex may function as a eukaryotic reverse gyrase introducing positive supercoils into extrachromosomal ribosomal DNA rings. Together with topoisomerase II has a role in chromosomal segregation. Maintains rDNA structure where it has a role in re-starting stalled replication forks.<ref>PMID:7969174</ref> <ref>PMID:7736577</ref> <ref>PMID:12228808</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: The HRDC (helicase and RNaseD C-terminal) domain is found at the C terminus of many RecQ helicases, including the human Werner and Bloom syndrome proteins. RecQ helicases have been shown to unwind DNA in an ATP-dependent manner. However, the specific functional roles of these proteins in DNA recombination and replication are not known. An HRDC domain exists in both of the human RecQ homologues that are implicated in human disease and may have an important role in their function. RESULTS: We have determined the three-dimensional structure of the HRDC domain in the Saccharomyces cerevisiae RecQ helicase Sgs1p by nuclear magnetic resonance (NMR) spectroscopy. The structure resembles auxiliary domains in bacterial DNA helicases and other proteins that interact with nucleic acids. We show that a positively charged region on the surface of the Sgs1p HRDC domain can interact with DNA. Structural similarities to bacterial DNA helicases suggest that the HRDC domain functions as an auxiliary domain in RecQ helicases. Homology models of the Werner and Bloom HRDC domains show different surface properties when compared with Sgs1p. CONCLUSIONS: The HRDC domain represents a structural scaffold that resembles auxiliary domains in proteins that are involved in nucleic acid metabolism. In Sgs1p, the HRDC domain could modulate the helicase function via auxiliary contacts to DNA. However, in the Werner and Bloom syndrome helicases the HRDC domain may have a role in their functional differences by mediating diverse molecular interactions.


==Overview==
The three-dimensional structure of the HRDC domain and implications for the Werner and Bloom syndrome proteins.,Liu Z, Macias MJ, Bottomley MJ, Stier G, Linge JP, Nilges M, Bork P, Sattler M Structure. 1999 Dec 15;7(12):1557-66. PMID:10647186<ref>PMID:10647186</ref>
BACKGROUND: The HRDC (helicase and RNaseD C-terminal) domain is found at the C terminus of many RecQ helicases, including the human Werner and Bloom syndrome proteins. RecQ helicases have been shown to unwind DNA in an ATP-dependent manner. However, the specific functional roles of these proteins in DNA recombination and replication are not known. An HRDC domain exists in both of the human RecQ homologues that are implicated in human disease and may have an important role in their function. RESULTS: We have determined the three-dimensional structure of the HRDC domain in the Saccharomyces cerevisiae RecQ helicase Sgs1p by nuclear magnetic resonance (NMR) spectroscopy. The structure resembles auxiliary domains in bacterial DNA helicases and other proteins that interact with nucleic acids. We show that a positively charged region on the surface of the Sgs1p HRDC domain can interact with DNA. Structural similarities to bacterial DNA helicases suggest that the HRDC domain functions as an auxiliary domain in RecQ helicases. Homology models of the Werner and Bloom HRDC domains show different surface properties when compared with Sgs1p. CONCLUSIONS: The HRDC domain represents a structural scaffold that resembles auxiliary domains in proteins that are involved in nucleic acid metabolism. In Sgs1p, the HRDC domain could modulate the helicase function via auxiliary contacts to DNA. However, in the Werner and Bloom syndrome helicases the HRDC domain may have a role in their functional differences by mediating diverse molecular interactions.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1D8B is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D8B OCA].
</div>
<div class="pdbe-citations 1d8b" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
The three-dimensional structure of the HRDC domain and implications for the Werner and Bloom syndrome proteins., Liu Z, Macias MJ, Bottomley MJ, Stier G, Linge JP, Nilges M, Bork P, Sattler M, Structure. 1999 Dec 15;7(12):1557-66. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10647186 10647186]
*[[Helicase 3D structures|Helicase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Bork P]]
[[Category: Bork, P.]]
[[Category: Bottomley MJ]]
[[Category: Bottomley, M J.]]
[[Category: Linge JP]]
[[Category: Linge, J P.]]
[[Category: Liu Z]]
[[Category: Liu, Z.]]
[[Category: Macias MJ]]
[[Category: Macias, M J.]]
[[Category: Nilges M]]
[[Category: Nilges, M.]]
[[Category: Sattler M]]
[[Category: Sattler, M.]]
[[Category: Stier G]]
[[Category: Stier, G.]]
[[Category: Five helice]]
[[Category: Three-helical bundle flanked by two helice]]
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