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PDBsum entry 6lts

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protein dna_rna metals Protein-protein interface(s) links
Transcription PDB id
6lts

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
226 a.a.
1111 a.a.
1486 a.a.
94 a.a.
336 a.a.
DNA/RNA
Metals
_MG ×5
_ZN ×2
PDB id:
6lts
Name: Transcription
Title: Crystal structure of thermus thermophilus transcription initiation complex comprising a truncated sigma finger
Structure: DNA-directed RNA polymerase subunit alpha. Chain: a, b. Synonym: rnap subunit alpha,RNA polymerase subunit alpha, transcriptase subunit alpha. DNA-directed RNA polymerase subunit beta. Chain: c. Synonym: rnap subunit beta,RNA polymerase subunit beta,transcriptase subunit beta. DNA-directed RNA polymerase subunit beta'.
Source: Thermus thermophilus hb8. Organism_taxid: 300852. Strain: hb8. Gene: siga, ttha0532. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Thermus thermophilus. Organism_taxid: 274.
Resolution:
3.45Å     R-factor:   0.221     R-free:   0.258
Authors: Y.Zhang,R.H.Ebright
Key ref: L.Li et al. (2020). RNA extension drives a stepwise displacement of an initiation-factor structural module in initial transcription. Proc Natl Acad Sci U S A, 117, 5801-5809. PubMed id: 32127479 DOI: 10.1073/pnas.1920747117
Date:
23-Jan-20     Release date:   11-Mar-20    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q5SHR6  (RPOA_THET8) -  DNA-directed RNA polymerase subunit alpha from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Seq:
Struc:
315 a.a.
226 a.a.
Protein chain
Pfam   ArchSchema ?
Q8RQE9  (RPOB_THET8) -  DNA-directed RNA polymerase subunit beta from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1119 a.a.
1111 a.a.
Protein chain
Pfam   ArchSchema ?
Q8RQE8  (RPOC_THET8) -  DNA-directed RNA polymerase subunit beta' from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1524 a.a.
1486 a.a.
Protein chain
Pfam   ArchSchema ?
Q8RQE7  (RPOZ_THET8) -  DNA-directed RNA polymerase subunit omega from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Seq:
Struc:
99 a.a.
94 a.a.
Protein chain
Pfam   ArchSchema ?
Q5SKW1  (Q5SKW1_THET8) -  RNA polymerase sigma factor SigA from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
Seq:
Struc:
423 a.a.
336 a.a.
Key:    PfamA domain  Secondary structure

DNA/RNA chains
  T-A-T-A-A-T-G-G-G-A-G-C-T-G-T-C-A-C-G-G-A-T-G-C 24 bases
  G-C-A-T-C-C-G-T-G-A 10 bases

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D, E: E.C.2.7.7.6  - DNA-directed Rna polymerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
RNA(n)
+ ribonucleoside 5'-triphosphate
= RNA(n+1)
+ diphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1073/pnas.1920747117 Proc Natl Acad Sci U S A 117:5801-5809 (2020)
PubMed id: 32127479  
 
 
RNA extension drives a stepwise displacement of an initiation-factor structural module in initial transcription.
L.Li, V.Molodtsov, W.Lin, R.H.Ebright, Y.Zhang.
 
  ABSTRACT  
 
All organisms-bacteria, archaea, and eukaryotes-have a transcription initiation factor that contains a structural module that binds within the RNA polymerase (RNAP) active-center cleft and interacts with template-strand single-stranded DNA (ssDNA) in the immediate vicinity of the RNAP active center. This transcription initiation-factor structural module preorganizes template-strand ssDNA to engage the RNAP active center, thereby facilitating binding of initiating nucleotides and enabling transcription initiation from initiating mononucleotides. However, this transcription initiation-factor structural module occupies the path of nascent RNA and thus presumably must be displaced before or during initial transcription. Here, we report four sets of crystal structures of bacterial initially transcribing complexes that demonstrate and define details of stepwise, RNA-extension-driven displacement of the "σ-finger" of the bacterial transcription initiation factor σ. The structures reveal that-for both the primary σ-factor and extracytoplasmic (ECF) σ-factors, and for both 5'-triphosphate RNA and 5'-hydroxy RNA-the "σ-finger" is displaced in stepwise fashion, progressively folding back upon itself, driven by collision with the RNA 5'-end, upon extension of nascent RNA from ∼5 nt to ∼10 nt.
 

 

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