PDBsum entry 3lpe

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protein metals Protein-protein interface(s) links
Transferase PDB id
Protein chains
84 a.a. *
59 a.a. *
_ZN ×4
Waters ×349
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure of spt4/5ngn heterodimer complex from meth jannaschii
Structure: Putative transcription antitermination protein nu chain: a, c, e, g. Fragment: ngn domain. Synonym: transcription elongation factor spt5 ngn. Engineered: yes. DNA-directed RNA polymerase subunit e''. Chain: b, d, f, h. Synonym: transcription elongation factor spt4. Engineered: yes
Source: Methanocaldococcus jannaschii. Methanococcus jannaschii. Organism_taxid: 2190. Gene: mj0372. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: rpoe2, mj0396.
1.90Å     R-factor:   0.210     R-free:   0.255
Authors: A.Hirtreiter,G.E.Damsma,A.C.M.Cheung,D.Klose,D.Grohmann,E.Vo A.C.R.Martin,P.Cramer,F.Werner
Key ref: A.Hirtreiter et al. (2010). Spt4/5 stimulates transcription elongation through the RNA polymerase clamp coiled-coil motif. Nucleic Acids Res, 38, 4040-4051. PubMed id: 20197319
05-Feb-10     Release date:   09-Mar-10    
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Protein chains
Pfam   ArchSchema ?
Q57818  (NUSG_METJA) -  Transcription elongation factor Spt5
147 a.a.
84 a.a.
Protein chains
Pfam   ArchSchema ?
Q57839  (RPOE2_METJA) -  Transcription elongation factor Spt4
59 a.a.
59 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     transcription, DNA-dependent   2 terms 
  Biochemical function     translation elongation factor activity     3 terms  


Nucleic Acids Res 38:4040-4051 (2010)
PubMed id: 20197319  
Spt4/5 stimulates transcription elongation through the RNA polymerase clamp coiled-coil motif.
A.Hirtreiter, G.E.Damsma, A.C.Cheung, D.Klose, D.Grohmann, E.Vojnic, A.C.Martin, P.Cramer, F.Werner.
Spt5 is the only known RNA polymerase-associated factor that is conserved in all three domains of life. We have solved the structure of the Methanococcus jannaschii Spt4/5 complex by X-ray crystallography, and characterized its function and interaction with the archaeal RNAP in a wholly recombinant in vitro transcription system. Archaeal Spt4 and Spt5 form a stable complex that associates with RNAP independently of the DNA-RNA scaffold of the elongation complex. The association of Spt4/5 with RNAP results in a stimulation of transcription processivity, both in the absence and the presence of the non-template strand. A domain deletion analysis reveals the molecular anatomy of Spt4/5--the Spt5 Nus-G N-terminal (NGN) domain is the effector domain of the complex that both mediates the interaction with RNAP and is essential for its elongation activity. Using a mutagenesis approach, we have identified a hydrophobic pocket on the Spt5 NGN domain as binding site for RNAP, and reciprocally the RNAP clamp coiled-coil motif as binding site for Spt4/5.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21187417 B.J.Klein, D.Bose, K.J.Baker, Z.M.Yusoff, X.Zhang, and K.S.Murakami (2011).
RNA polymerase and transcription elongation factor Spt4/5 complex structure.
  Proc Natl Acad Sci U S A, 108, 546-550.
PDB code: 3p8b
21386817 F.W.Martinez-Rucobo, S.Sainsbury, A.C.Cheung, and P.Cramer (2011).
Architecture of the RNA polymerase-Spt4/5 complex and basis of universal transcription processivity.
  EMBO J, 30, 1302-1310.
PDB code: 3qqc
21233849 F.Werner, and D.Grohmann (2011).
Evolution of multisubunit RNA polymerases in the three domains of life.
  Nat Rev Microbiol, 9, 85-98.  
21478900 T.J.Santangelo, and I.Artsimovitch (2011).
Termination and antitermination: RNA polymerase runs a stop sign.
  Nat Rev Microbiol, 9, 319-329.  
20818391 A.Mayer, M.Lidschreiber, M.Siebert, K.Leike, J.Söding, and P.Cramer (2010).
Uniform transitions of the general RNA polymerase II transcription complex.
  Nat Struct Mol Biol, 17, 1272-1278.  
20639538 A.Sevostyanova, and I.Artsimovitch (2010).
Functional analysis of Thermus thermophilus transcription factor NusG.
  Nucleic Acids Res, 38, 7432-7445.  
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