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PDBsum entry 2qb1

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protein Protein-protein interface(s) links
Hydrolase regulator PDB id
2qb1
Jmol
Contents
Protein chains
78 a.a. *
Waters ×4
* Residue conservation analysis
PDB id:
2qb1
Name: Hydrolase regulator
Title: 2tel crystallization module
Structure: E80-telsam domain. Chain: a, b. Engineered: yes
Source: Escherichia coli. Expressed in: escherichia coli
Resolution:
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
Date:
15-Jun-07     Release date:   14-Oct-08    
PROCHECK
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 Headers
 References

Protein chains
No UniProt id for this chain
Struc: 78 a.a.
Key:    Secondary structure  CATH domain

 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.
 
  ABSTRACT  
 
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.  
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.