spacer
spacer

PDBsum entry 2wnm

Go to PDB code: 
protein links
Hydrolase PDB id
2wnm

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chain
59 a.a. *
* Residue conservation analysis
PDB id:
2wnm
Name: Hydrolase
Title: Solution structure of gp2
Structure: Gene 2. Chain: a. Synonym: gp2. Engineered: yes
Source: Enterobacteria phage t7. Organism_taxid: 10760. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 1 models
Authors: B.Camara,M.Liu,A.Shadrinc,B.Liu,P.Simpson,R.Weinzierl,K.Severinovc, E.Cota,S.Matthews,S.R.Wigneshweraraj
Key ref: B.Cámara et al. (2010). T7 phage protein Gp2 inhibits the Escherichia coli RNA polymerase by antagonizing stable DNA strand separation near the transcription start site. Proc Natl Acad Sci U S A, 107, 2247-2252. PubMed id: 20133868
Date:
13-Jul-09     Release date:   16-Feb-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P03704  (VRPI_BPT7) -  Bacterial RNA polymerase inhibitor from Escherichia phage T7
Seq:
Struc:
64 a.a.
59 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
Proc Natl Acad Sci U S A 107:2247-2252 (2010)
PubMed id: 20133868  
 
 
T7 phage protein Gp2 inhibits the Escherichia coli RNA polymerase by antagonizing stable DNA strand separation near the transcription start site.
B.Cámara, M.Liu, J.Reynolds, A.Shadrin, B.Liu, K.Kwok, P.Simpson, R.Weinzierl, K.Severinov, E.Cota, S.Matthews, S.R.Wigneshweraraj.
 
  ABSTRACT  
 
Infection of Escherichia coli by the T7 phage leads to rapid and selective inhibition of the host RNA polymerase (RNAP)--a multi-subunit enzyme responsible for gene transcription--by a small ( approximately 7 kDa) phage-encoded protein called Gp2. Gp2 is also a potent inhibitor of E. coli RNAP in vitro. Here we describe the first atomic resolution structure of Gp2, which reveals a distinct run of surface-exposed negatively charged amino acid residues on one side of the molecule. Our comprehensive mutagenesis data reveal that two conserved arginine residues located on the opposite side of Gp2 are important for binding to and inhibition of RNAP. Based on a structural model of the Gp2-RNAP complex, we propose that inhibition of transcription by Gp2 involves prevention of RNAP-promoter DNA interactions required for stable DNA strand separation and maintenance of the "transcription bubble" near the transcription start site, an obligatory step in the formation of a transcriptionally competent promoter complex.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21316373 C.Sheppard, B.Cámara, A.Shadrin, N.Akulenko, M.Liu, G.Baldwin, K.Severinov, E.Cota, S.Matthews, and S.R.Wigneshweraraj (2011).
Inhibition of Escherichia coli RNAp by T7 Gp2 protein: role of negatively charged strip of amino acid residues in Gp2.
  J Mol Biol, 407, 623-632.  
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.

 

spacer

spacer