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| | <StructureSection load='2fzl' size='340' side='right'caption='[[2fzl]], [[Resolution|resolution]] 2.90Å' scene=''> | | <StructureSection load='2fzl' size='340' side='right'caption='[[2fzl]], [[Resolution|resolution]] 2.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2fzl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfl Arcfl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FZL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FZL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2fzl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FZL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FZL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></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]] 2.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2fwr|2fwr]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></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=2fzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fzl OCA], [http://pdbe.org/2fzl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fzl RCSB], [http://www.ebi.ac.uk/pdbsum/2fzl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fzl 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=2fzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fzl OCA], [https://pdbe.org/2fzl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fzl RCSB], [https://www.ebi.ac.uk/pdbsum/2fzl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fzl ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/O29889_ARCFU O29889_ARCFU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arcfl]] | + | [[Category: Archaeoglobus fulgidus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Arvai, A S]] | + | [[Category: Arvai AS]] |
| - | [[Category: Fan, L]] | + | [[Category: Fan L]] |
| - | [[Category: Tainer, J A]] | + | [[Category: Tainer JA]] |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Dna repair]]
| + | |
| - | [[Category: Nucleotide excision repair]]
| + | |
| - | [[Category: Xpb]]
| + | |
| Structural highlights
Function
O29889_ARCFU
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 PubMed
The 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
- ↑ Fan L, Arvai AS, Cooper PK, Iwai S, Hanaoka F, Tainer JA. Conserved XPB core structure and motifs for DNA unwinding: implications for pathway selection of transcription or excision repair. Mol Cell. 2006 Apr 7;22(1):27-37. PMID:16600867 doi:http://dx.doi.org/10.1016/j.molcel.2006.02.017
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