PDBsum entry 2qb1

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protein Protein-protein interface(s) links
Hydrolase regulator PDB id
Protein chains
78 a.a. *
Waters ×4
* Residue conservation analysis
PDB id:
Name: Hydrolase regulator
Title: 2tel crystallization module
Structure: E80-telsam domain. Chain: a, b. Engineered: yes
Source: Escherichia coli. Expressed in: escherichia coli
2.61Å     R-factor:   0.212     R-free:   0.241
Authors: S.Nauli,J.U.Bowie
Key ref:
S.Nauli et al. (2007). Polymer-driven crystallization. Protein Sci, 16, 2542-2551. PubMed id: 17962407 DOI: 10.1110/ps.073074207
15-Jun-07     Release date:   14-Oct-08    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P41212  (ETV6_HUMAN) -  Transcription factor ETV6
452 a.a.
78 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   1 term 
  Biochemical function     sequence-specific DNA binding     1 term  


DOI no: 10.1110/ps.073074207 Protein Sci 16:2542-2551 (2007)
PubMed id: 17962407  
Polymer-driven crystallization.
S.Nauli, S.Farr, Y.J.Lee, H.Y.Kim, S.Faham, J.U.Bowie.
Obtaining well-diffracting crystals of macromolecules remains a significant barrier to structure determination. Here we propose and test a new approach to crystallization, in which the crystallization target is fused to a polymerizing protein module, so that polymer formation drives crystallization of the target. We test the approach using a polymerization module called 2TEL, which consists of two tandem sterile alpha motif (SAM) domains from the protein translocation Ets leukemia (TEL). The 2TEL module is engineered to polymerize as the pH is lowered, which allows the subtle modulation of polymerization needed for crystal formation. We show that the 2TEL module can drive the crystallization of 11 soluble proteins, including three that resisted prior crystallization attempts. In addition, the 2TEL module crystallizes in the presence of various detergents, suggesting that it might facilitate membrane protein crystallization. The crystal structures of two fusion proteins show that the TELSAM polymer is responsible for the majority of contacts in the crystal lattice. The results suggest that biological polymers could be designed as crystallization modules.
  Selected figure(s)  
Figure 4.
Figure 4. Crystal structures and packing of the 2TEL module (sticks model) fused to T4 lysozyme (ribbon diagram) viewed down the
  The above figure is reprinted by permission from the Protein Society: Protein Sci (2007, 16, 2542-2551) copyright 2007.  
  Figure was selected by the author.  
    Author's comment    
  The figure shows the crystal contacts observed for a fusion protein containing the 2TEL crystallization module and T4-lysozyme.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21217644 A.M.Grabrucker, M.J.Knight, C.Proepper, J.Bockmann, M.Joubert, M.Rowan, G.U.Nienhaus, C.C.Garner, J.U.Bowie, M.R.Kreutz, E.D.Gundelfinger, and T.M.Boeckers (2011).
Concerted action of zinc and ProSAP/Shank in synaptogenesis and synapse maturation.
  EMBO J, 30, 569-581.  
21082721 G.J.Forse, N.Ram, D.R.Banatao, D.Cascio, M.R.Sawaya, H.E.Klock, S.A.Lesley, and T.O.Yeates (2011).
Synthetic symmetrization in the crystallization and structure determination of CelA from Thermotoga maritima.
  Protein Sci, 20, 168-178.
PDB code: 3o7o
20445236 Z.S.Derewenda (2010).
Application of protein engineering to enhance crystallizability and improve crystal properties.
  Acta Crystallogr D Biol Crystallogr, 66, 604-615.  
19477632 S.Koide (2009).
Engineering of recombinant crystallization chaperones.
  Curr Opin Struct Biol, 19, 449-457.  
18780816 L.Corsini, M.Hothorn, K.Scheffzek, M.Sattler, and G.Stier (2008).
Thioredoxin as a fusion tag for carrier-driven crystallization.
  Protein Sci, 17, 2070-2079.  
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