2QB0
Structure of the 2TEL crystallization module fused to T4 lysozyme with an Ala-Gly-Pro linker.
Summary for 2QB0
| Entry DOI | 10.2210/pdb2qb0/pdb |
| Related | 2QAR 2QB1 |
| Descriptor | Transcription factor ETV6, Transcription factor ETV6,Endolysin, MANGANESE (II) ION, ... (4 entities in total) |
| Functional Keywords | helical polymer, hydrolase regulator |
| Biological source | Homo sapiens More |
| Cellular location | Host cytoplasm : P41212 |
| Total number of polymer chains | 4 |
| Total formula weight | 74221.30 |
| Authors | Nauli, S.,Bowie, J.U. (deposition date: 2007-06-15, release date: 2008-10-14, Last modification date: 2024-02-21) |
| Primary citation | Nauli, S.,Farr, S.,Lee, Y.J.,Kim, H.Y.,Faham, S.,Bowie, J.U. Polymer-driven crystallization. Protein Sci., 16:2542-2551, 2007 Cited by PubMed 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. PubMed: 17962407DOI: 10.1110/ps.073074207 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.56 Å) |
Structure validation
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