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PDBsum entry 3lpe

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protein metals Protein-protein interface(s) links
Transferase PDB id
3lpe
Jmol
Contents
Protein chains
84 a.a. *
59 a.a. *
Metals
_ZN ×4
Waters ×349
* Residue conservation analysis
PDB id:
3lpe
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.
Resolution:
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
Date:
05-Feb-10     Release date:   09-Mar-10    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q57818  (NUSG_METJA) -  Transcription elongation factor Spt5
Seq:
Struc:
147 a.a.
84 a.a.
Protein chains
Pfam   ArchSchema ?
Q57839  (RPOE2_METJA) -  Transcription elongation factor Spt4
Seq:
Struc:
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.
 
  ABSTRACT  
 
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.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.