5h8c
From Proteopedia
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==Truncated XPD== | ==Truncated XPD== | ||
<StructureSection load='5h8c' size='340' side='right' caption='[[5h8c]], [[Resolution|resolution]] 2.29Å' scene=''> | <StructureSection load='5h8c' size='340' side='right' caption='[[5h8c]], [[Resolution|resolution]] 2.29Å' scene=''> | ||
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<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=5h8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h8c OCA], [http://pdbe.org/5h8c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h8c RCSB], [http://www.ebi.ac.uk/pdbsum/5h8c PDBsum]</span></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=5h8c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h8c OCA], [http://pdbe.org/5h8c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h8c RCSB], [http://www.ebi.ac.uk/pdbsum/5h8c PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The xeroderma pigmentosum group D (XPD) helicase is a component of the transcription factor IIH complex in eukaryotes and plays an essential role in DNA repair in the nucleotide excision repair pathway. XPD is a 5' to 3' helicase with an essential iron-sulfur cluster. Structural and biochemical studies of the monomeric archaeal XPD homologues have aided a mechanistic understanding of this important class of helicase, but several important questions remain open. In particular, the mechanism for DNA loading, which is assumed to require large protein conformational change, is not fully understood. Here, DNA binding by the archaeal XPD helicase from Thermoplasma acidophilum has been investigated using a combination of crystallography, cross-linking, modified substrates and biochemical assays. The data are consistent with an initial tight binding of ssDNA to helicase domain 2, followed by transient opening of the interface between the Arch and 4FeS domains, allowing access to a second binding site on helicase domain 1 that directs DNA through the pore. A crystal structure of XPD from Sulfolobus acidocaldiarius that lacks helicase domain 2 has an otherwise unperturbed structure, emphasizing the stability of the interface between the Arch and 4FeS domains in XPD. | ||
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| + | Mechanism of DNA loading by the DNA repair helicase XPD.,Constantinescu-Aruxandei D, Petrovic-Stojanovska B, Penedo JC, White MF, Naismith JH Nucleic Acids Res. 2016 Feb 20. pii: gkw102. PMID:26896802<ref>PMID:26896802</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5h8c" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 06:56, 2 March 2016
Truncated XPD
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