PDBsum entry 2rvb

DNA binding protein/transcription

PDB id: 2rvb

Contents

Protein chains

48 a.a.

108 a.a.

PDB id:

2rvb

Name:

DNA binding protein/transcription

Title:

Solution structure of the complex between xpc acidic domain and tfiih p62 ph domain

Structure:

DNA repair protein complementing xp-c cells. Chain: a. Synonym: xeroderma pigmentosum group c-complementing protein, p125. Engineered: yes. General transcription factor iih subunit 1. Chain: b. Synonym: basic transcription factor 2 62 kda subunit, btf2 p62, general transcription factor iih polypeptide 1, tfiih basal transcription factor complex p62 subunit.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: xpc, xpcc. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: gtf2h1, btf2.

NMR struc:

20 models

Authors:

M.Okuda,Y.Nishimura

Key ref:

M.Okuda et al. (2015). Structural Insight into the Mechanism of TFIIH Recognition by the Acidic String of the Nucleotide Excision Repair Factor XPC. Structure, 23, 1827-1837. PubMed id: 26278177 DOI: 10.1016/j.str.2015.07.009

Date:

01-Jul-15 Release date: 09-Sep-15

Protein chain

Q01831  (XPC_HUMAN) -  DNA repair protein complementing XP-C cells from Homo sapiens

Seq: 940 a.a.

Struc: 48 a.a.

Protein chain

P32780  (TF2H1_HUMAN) -  General transcription factor IIH subunit 1 from Homo sapiens

Seq: 548 a.a.

Struc: 108 a.a.

Enzyme reactions

• Enzyme class: Chains A, B: E.C.?

DOI no: 10.1016/j.str.2015.07.009

Structure 23:1827-1837 (2015)

PubMed id: 26278177

Structural Insight into the Mechanism of TFIIH Recognition by the Acidic String of the Nucleotide Excision Repair Factor XPC.

M.Okuda, M.Kinoshita, E.Kakumu, K.Sugasawa, Y.Nishimura.

ABSTRACT

In global genome repair (GGR), XPC detects damaged nucleotides and recruits TFIIH complex. The small acidic region of XPC binds to the pleckstrin homology (PH) domain of TFIIH subunit p62; however, the recognition mechanism remains elusive. Here, we use nuclear magnetic resonance to present the tertiary structure of XPC bound to the PH domain. The XPC acidic region forms a long string stabilized by insertion of Trp133 and Val136 into two separate hollows of the PH domain, coupled with extensive electrostatic contacts. Analysis of several XPC mutants revealed that particularly Trp133 is essential for binding to the PH domain. In cell lines stably expressing mutant XPC, alanine substitution at Trp133 or Trp133/Val136 compromised UV resistance, recruitment of TFIIH to DNA damage, and removal of UV-induced photoproducts from genomic DNA. These findings show how TFIIH complex is recruited by XPC to damaged DNA, advancing our understanding of the early stage of GGR.