2fz4: Difference between revisions
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==Crystal Structure of the N-terminal half of Archaeoglobus Fulgidus XPB== | ==Crystal Structure of the N-terminal half of Archaeoglobus Fulgidus XPB== | ||
<StructureSection load='2fz4' size='340' side='right' caption='[[2fz4]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2fz4' size='340' side='right' caption='[[2fz4]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
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<table><tr><td colspan='2'>[[2fz4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfu Arcfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FZ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FZ4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2fz4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfu Arcfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FZ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FZ4 FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAD25 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224325 ARCFU])</td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RAD25 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224325 ARCFU])</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=2fz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fz4 OCA], [http://pdbe.org/2fz4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fz4 RCSB], [http://www.ebi.ac.uk/pdbsum/2fz4 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=2fz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fz4 OCA], [http://pdbe.org/2fz4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fz4 RCSB], [http://www.ebi.ac.uk/pdbsum/2fz4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fz4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fz/2fz4_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fz/2fz4_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 10:07, 20 June 2018
Crystal Structure of the N-terminal half of Archaeoglobus Fulgidus XPBCrystal Structure of the N-terminal half of Archaeoglobus Fulgidus XPB
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe human xeroderma pigmentosum group B (XPB) helicase is essential for transcription, nucleotide excision repair, and TFIIH functional assembly. Here, we determined crystal structures of an Archaeoglobus fulgidus XPB homolog (AfXPB) that characterize two RecA-like XPB helicase domains and discover a DNA damage recognition domain (DRD), a unique RED motif, a flexible thumb motif (ThM), and implied conformational changes within a conserved functional core. RED motif mutations dramatically reduce helicase activity, and the DRD and ThM, which flank the RED motif, appear structurally as well as functionally analogous to the MutS mismatch recognition and DNA polymerase thumb domains. Substrate specificity is altered by DNA damage, such that AfXPB unwinds dsDNA with 3' extensions, but not blunt-ended dsDNA, unless it contains a lesion, as shown for CPD or (6-4) photoproducts. Together, these results provide an unexpected mechanism of DNA unwinding with implications for XPB damage verification in nucleotide excision repair. Conserved XPB core structure and motifs for DNA unwinding: implications for pathway selection of transcription or excision repair.,Fan L, Arvai AS, Cooper PK, Iwai S, Hanaoka F, Tainer JA Mol Cell. 2006 Apr 7;22(1):27-37. PMID:16600867[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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