1OMS
Structure determination by MAD: E.coli Trigger Factor binding at the ribosomal exit tunnel.
Summary for 1OMS
| Entry DOI | 10.2210/pdb1oms/pdb |
| Descriptor | Trigger Factor, SULFATE ION, TETRAETHYLENE GLYCOL, ... (6 entities in total) |
| Functional Keywords | alpha-beta structure, isomerase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 3 |
| Total formula weight | 42890.83 |
| Authors | Kristensen, O.,Gajhede, M. (deposition date: 2003-02-26, release date: 2003-12-16, Last modification date: 2011-07-13) |
| Primary citation | Kristensen, O.,Gajhede, M. Chaperone binding at the ribosomal exit tunnel. Structure, 11:1547-1556, 2003 Cited by PubMed Abstract: The exit tunnel region of the ribosome is well established as a focal point for interaction between the components that guide the fate of nascent polypeptides. One of these, the chaperone trigger factor (TF), associates with the 50S ribosomal subunit through its N-terminal domain. Targeting of TF to ribosomes is crucial to achieve its remarkable efficiency in protein folding. A similar tight coupling to translation is found in signal recognition particle (SRP)-dependent protein translocation. Here, we report crystal structures of the E. coli TF ribosome binding domain. TF is structurally related to the Hsp33 chaperone but has a prominent ribosome anchor located as a tip of the molecule. This tip includes the previously established unique TF signature motif. Comparison reveals that this feature is not found in SRP structures. We identify a conserved helical kink as a hallmark of the TF structure that is most likely critical to ensure ribosome association. PubMed: 14656439DOI: 10.1016/j.str.2003.11.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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