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PDBsum entry 5ivw

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protein dna_rna Protein-protein interface(s) links
Transcription/DNA PDB id
5ivw

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
475 a.a.
665 a.a.
188 a.a.
62 a.a.
274 a.a.
193 a.a.
DNA/RNA
PDB id:
5ivw
Name: Transcription/DNA
Title: Human core tfiih bound to DNA within the pic
Structure: Tfiih basal transcription factor complex helicase xpb subunit. Chain: v. Synonym: basic transcription factor 2 89 kda subunit, btf2 p89, DNA excision repair protein ercc-3, DNA repair protein complementing xp-b cells, tfiih basal transcription factor complex 89 kda subunit, tfiih p89, xeroderma pigmentosum group b-complementing protein. Tfiih basal transcription factor complex helicase xpd subunit.
Source: Homo sapiens. Human. Organism_taxid: 9606. Synthetic: yes. Organism_taxid: 9606
Authors: Y.He,C.Yan,J.Fang,C.Inouye,R.Tjian,I.Ivanov,E.Nogales
Key ref: Y.He et al. (2016). Near-atomic resolution visualization of human transcription promoter opening. Nature, 533, 359-365. PubMed id: 27193682 DOI: 10.1038/nature17970
Date:
21-Mar-16     Release date:   18-May-16    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P19447  (ERCC3_HUMAN) -  General transcription and DNA repair factor IIH helicase subunit XPB from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
782 a.a.
475 a.a.
Protein chain
Pfam   ArchSchema ?
P18074  (ERCC2_HUMAN) -  General transcription and DNA repair factor IIH helicase subunit XPD from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
760 a.a.
665 a.a.
Protein chain
Pfam   ArchSchema ?
Q13888  (TF2H2_HUMAN) -  General transcription factor IIH subunit 2 from Homo sapiens
Seq:
Struc:
395 a.a.
188 a.a.
Protein chain
Pfam   ArchSchema ?
Q6ZYL4  (TF2H5_HUMAN) -  General transcription factor IIH subunit 5 from Homo sapiens
Seq:
Struc:
71 a.a.
62 a.a.
Protein chain
Pfam   ArchSchema ?
Q92759  (TF2H4_HUMAN) -  General transcription factor IIH subunit 4 from Homo sapiens
Seq:
Struc:
462 a.a.
274 a.a.
Protein chain
Pfam   ArchSchema ?
Q13889  (TF2H3_HUMAN) -  General transcription factor IIH subunit 3 from Homo sapiens
Seq:
Struc:
308 a.a.
193 a.a.
Key:    PfamA domain  Secondary structure

DNA/RNA chains
  A-T-T-G-C-C-G-A-A-G-A-C-G-A-A-A-A-A-A 19 bases
  T-T-T-T-T-T-T-C-G-T-C-T-T-C-G-G-C-A-A-T 20 bases

 Enzyme reactions 
   Enzyme class 1: Chains 0, 1, 2, 3: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
   Enzyme class 2: Chains V, W: E.C.3.6.4.12  - Dna helicase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O = ADP + phosphate + H+
ATP
+ H2O
= ADP
+ phosphate
+ H(+)
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1038/nature17970 Nature 533:359-365 (2016)
PubMed id: 27193682  
 
 
Near-atomic resolution visualization of human transcription promoter opening.
Y.He, C.Yan, J.Fang, C.Inouye, R.Tjian, I.Ivanov, E.Nogales.
 
  ABSTRACT  
 
In eukaryotic transcription initiation, a large multi-subunit pre-initiation complex (PIC) that assembles at the core promoter is required for the opening of the duplex DNA and identification of the start site for transcription by RNA polymerase II. Here we use cryo-electron microscropy (cryo-EM) to determine near-atomic resolution structures of the human PIC in a closed state (engaged with duplex DNA), an open state (engaged with a transcription bubble), and an initially transcribing complex (containing six base pairs of DNA-RNA hybrid). Our studies provide structures for previously uncharacterized components of the PIC, such as TFIIE and TFIIH, and segments of TFIIA, TFIIB and TFIIF. Comparison of the different structures reveals the sequential conformational changes that accompany the transition from each state to the next throughout the transcription initiation process. This analysis illustrates the key role of TFIIB in transcription bubble stabilization and provides strong structural support for a translocase activity of XPB.
 

 

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