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PDBsum entry 5jjk

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protein dna_rna ligands metals Protein-protein interface(s) links
Transcription/RNA PDB id
5jjk

 

 

 

 

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Contents
Protein chains
405 a.a.
356 a.a.
DNA/RNA
Ligands
ADP ×6
BEF ×6
Metals
_MG ×6
Waters ×19
PDB id:
5jjk
Name: Transcription/RNA
Title: Rho transcription termination factor bound to ra7 and 6 adp-bef3 molecules
Structure: Transcription termination factor rho. Chain: a, b, c, d, e, f. Synonym: atp-dependent helicase rho. Engineered: yes. Mutation: yes. Ra12: RNA (5'-r(p Ap Ap Ap Ap Ap Ap A)-3'). Chain: g. Engineered: yes
Source: Escherichia coli o157:h7. Organism_taxid: 83334. Gene: rho, z5293, ecs4716. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Synthetic construct. Organism_taxid: 32630
Resolution:
3.15Å     R-factor:   0.235     R-free:   0.265
Authors: N.D.Thomsen,M.R.Lawson,L.B.Witkowsky,S.Qu,J.M.Berger
Key ref: N.D.Thomsen et al. (2016). Molecular mechanisms of substrate-controlled ring dynamics and substepping in a nucleic acid-dependent hexameric motor. Proc Natl Acad Sci U S A, 113, E7691. PubMed id: 27856760 DOI: 10.1073/pnas.1616745113
Date:
24-Apr-16     Release date:   16-Nov-16    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0AG30  (RHO_ECOLI) -  Transcription termination factor Rho from Escherichia coli (strain K12)
Seq:
Struc:
419 a.a.
405 a.a.
Protein chain
Pfam   ArchSchema ?
P0AG30  (RHO_ECOLI) -  Transcription termination factor Rho from Escherichia coli (strain K12)
Seq:
Struc:
419 a.a.
356 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

DNA/RNA chain
  A-A-A-A-A-A-A 7 bases

 Enzyme reactions 
   Enzyme class: Chains A, B, C, D, E, F: E.C.3.6.4.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1073/pnas.1616745113 Proc Natl Acad Sci U S A 113:E7691 (2016)
PubMed id: 27856760  
 
 
Molecular mechanisms of substrate-controlled ring dynamics and substepping in a nucleic acid-dependent hexameric motor.
N.D.Thomsen, M.R.Lawson, L.B.Witkowsky, S.Qu, J.M.Berger.
 
  ABSTRACT  
 
No abstract given.

 

 

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