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PDBsum entry 2fkd

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protein Protein-protein interface(s) links
Transcription regulator PDB id
2fkd

 

 

 

 

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Contents
Protein chains
(+ 8 more) 110 a.a. *
* Residue conservation analysis
PDB id:
2fkd
Name: Transcription regulator
Title: Crystal structure of thE C-terminal domain of bacteriophage 186 repressor
Structure: Repressor protein ci. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n. Fragment: c-terminal domain. Engineered: yes
Source: Enterobacteria phage 186. Organism_taxid: 29252. Gene: ci. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: 40mer (from PQS)
Resolution:
2.70Å     R-factor:   0.240     R-free:   0.297
Authors: M.Lewis
Key ref:
H.W.Pinkett et al. (2006). The structural basis of cooperative regulation at an alternate genetic switch. Mol Cell, 21, 605-615. PubMed id: 16507359 DOI: 10.1016/j.molcel.2006.01.019
Date:
04-Jan-06     Release date:   13-Jun-06    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P08707  (RPC1_BP186) -  Repressor protein CI from Escherichia phage 186
Seq:
Struc:
192 a.a.
110 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

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

 

 
DOI no: 10.1016/j.molcel.2006.01.019 Mol Cell 21:605-615 (2006)
PubMed id: 16507359  
 
 
The structural basis of cooperative regulation at an alternate genetic switch.
H.W.Pinkett, K.E.Shearwin, S.Stayrook, I.B.Dodd, T.Burr, A.Hochschild, J.B.Egan, M.Lewis.
 
  ABSTRACT  
 
Bacteriophage lambda is a paradigm for understanding the role of cooperativity in gene regulation. Comparison of the regulatory regions of lambda and the unrelated temperate bacteriophage 186 provides insight into alternate ways to assemble functional genetic switches. The structure of the C-terminal domain of the 186 repressor, determined at 2.7 A resolution, reveals an unusual heptamer of dimers, consistent with presented genetic studies. In addition, the structure of a cooperativity mutant of the full-length 186 repressor, identified by genetic screens, was solved to 1.95 A resolution. These structures provide a molecular basis for understanding lysogenic regulation in 186. Whereas the overall fold of the 186 and lambda repressor monomers is remarkably similar, the way the two repressors cooperatively assemble is quite different and explains in part the differences in their regulatory activity.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. Comparison of the λ and 186 Switch Regions
Figure 2.
Figure 2. Structures of the CTD of λ and 186 Repressor
 
  The above figures are reprinted by permission from Cell Press: Mol Cell (2006, 21, 605-615) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21245039 N.Hao, M.L.Whitelaw, K.E.Shearwin, I.B.Dodd, and A.Chapman-Smith (2011).
Identification of residues in the N-terminal PAS domains important for dimerization of Arnt and AhR.
  Nucleic Acids Res, 39, 3695-3709.  
20118255 M.Pedersen, M.Ligowska, and K.Hammer (2010).
Characterization of the CI repressor protein encoded by the temperate lactococcal phage TP901-1.
  J Bacteriol, 192, 2102-2110.  
20639540 T.Massad, K.Skaar, H.Nilsson, P.Damberg, P.Henriksson-Peltola, E.Haggård-Ljungquist, M.Högbom, and P.Stenmark (2010).
Crystal structure of the P2 C-repressor: a binder of non-palindromic direct DNA repeats.
  Nucleic Acids Res, 38, 7778-7790.
PDB code: 2xcj
17485481 A.Ahlgren-Berg, P.Henriksson-Peltola, W.Sehlén, and E.Haggård-Ljungquist (2007).
A comparison of the DNA binding and bending capacities and the oligomeric states of the immunity repressors of heteroimmune coliphages P2 and WPhi.
  Nucleic Acids Res, 35, 3167-3180.  
17412705 P.Henriksson-Peltola, W.Sehlén, and E.Haggård-Ljungquist (2007).
Determination of the DNA-binding kinetics of three related but heteroimmune bacteriophage repressors using EMSA and SPR analysis.
  Nucleic Acids Res, 35, 3181-3191.  
16934834 D.Ndjonka, and C.E.Bell (2006).
Structure of a hyper-cleavable monomeric fragment of phage lambda repressor containing the cleavage site region.
  J Mol Biol, 362, 479-489.
PDB codes: 2hnf 2ho0
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.

 

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