Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Lesion recognition by XPC, TFIIH and XPA in DNA excision repair.
Journal, issue, pages	Nature, Vol. 617, Issue 7959, Page 170-175, Year 2023
Publish date	Apr 19, 2023
Authors	Jinseok Kim / Chia-Lung Li / Xuemin Chen / Yanxiang Cui / Filip M Golebiowski / Huaibin Wang / Fumio Hanaoka / Kaoru Sugasawa / Wei Yang /
PubMed Abstract	Nucleotide excision repair removes DNA lesions caused by ultraviolet light, cisplatin-like compounds and bulky adducts. After initial recognition by XPC in global genome repair or a stalled RNA ...Nucleotide excision repair removes DNA lesions caused by ultraviolet light, cisplatin-like compounds and bulky adducts. After initial recognition by XPC in global genome repair or a stalled RNA polymerase in transcription-coupled repair, damaged DNA is transferred to the seven-subunit TFIIH core complex (Core7) for verification and dual incisions by the XPF and XPG nucleases. Structures capturing lesion recognition by the yeast XPC homologue Rad4 and TFIIH in transcription initiation or DNA repair have been separately reported. How two different lesion recognition pathways converge and how the XPB and XPD helicases of Core7 move the DNA lesion for verification are unclear. Here we report on structures revealing DNA lesion recognition by human XPC and DNA lesion hand-off from XPC to Core7 and XPA. XPA, which binds between XPB and XPD, kinks the DNA duplex and shifts XPC and the DNA lesion by nearly a helical turn relative to Core7. The DNA lesion is thus positioned outside of Core7, as would occur with RNA polymerase. XPB and XPD, which track the lesion-containing strand but translocate DNA in opposite directions, push and pull the lesion-containing strand into XPD for verification.
External links	Nature / PubMed:37076618 / PubMed Central
Methods	EM (single particle)
Resolution	3.3 - 7.1 Å
Structure data	27996 8ebs EMDB-27996, PDB-8ebs: Initial DNA-lesion (Cy5) binding by XPC and TFIIH Method: EM (single particle) / Resolution: 4.0 Å 27997 8ebt EMDB-27997, PDB-8ebt: XPA repositioning Core7 of TFIIH relative to XPC-DNA lesion (Cy5) Method: EM (single particle) / Resolution: 3.9 Å 27998 8ebu EMDB-27998, PDB-8ebu: XPC release from Core7-XPA-DNA (Cy5) Method: EM (single particle) / Resolution: 3.3 Å 27999 8ebv EMDB-27999, PDB-8ebv: Initial DNA-lesion (AP) binding by XPC and TFIIH complex 1 Method: EM (single particle) / Resolution: 7.1 Å 28000 8ebw EMDB-28000, PDB-8ebw: Initial DNA-lesion (AP) binding by XPC and TFIIH complex2 Method: EM (single particle) / Resolution: 5.6 Å 28001 8ebx EMDB-28001, PDB-8ebx: XPA repositioning Core7 of TFIIH relative to XPC-DNA lesion (AP) Method: EM (single particle) / Resolution: 3.6 Å 28002 8eby EMDB-28002, PDB-8eby: XPC release from Core7-XPA-DNA (AP) Method: EM (single particle) / Resolution: 3.6 Å EMDB-29673: Bulky DNA lesion recognition complex 3 Method: EM (single particle) / Resolution: 3.4 Å EMDB-29674: Initial DNA-lesion (Cy5) binding by XPC and TFIIH focused Method: EM (single particle) / Resolution: 4.2 Å
Chemicals	ChemComp-SF4: IRON/SULFUR CLUSTER / Iron–sulfur cluster ChemComp-ZN: Unknown entry ChemComp-CA: Unknown entry
Source	homo sapiens (human) synthetic construct (others)
Keywords	DNA BINDING PROTEIN/DNA / Protein-DNA complex / DNA BINDING PROTEIN-DNA complex