3EDC
Crystal Structure of a 1.6-hexanediol Bound Tetrameric Form of Escherichia coli Lac-repressor Refined to 2.1 Resolution
Summary for 3EDC
| Entry DOI | 10.2210/pdb3edc/pdb |
| Descriptor | Lactose operon repressor, HEXANE-1,6-DIOL (3 entities in total) |
| Functional Keywords | lac-repressor, allosteric, tetramer, dna-binding, repressor, transcription, transcription regulation |
| Biological source | Escherichia coli K12 |
| Total number of polymer chains | 4 |
| Total formula weight | 154980.79 |
| Authors | Stenberg, K.A.E. (deposition date: 2008-09-03, release date: 2008-11-25, Last modification date: 2023-11-01) |
| Primary citation | Stenberg, K.A.E.,Vihinen, M. Crystal structure of a 1.6-hexanediol bound tetrameric form of Escherichia coli lac-repressor refined to 2.1 A resolution Proteins, 75:748-759, 2009 Cited by PubMed Abstract: We report the structure of a novel tetrameric form of the lactose repressor (LacI) protein from Escherichia coli refined to 2.1 A resolution. The tetramer is bound to 1.6-hexanediol present in the crystallization solution and the final R(free) for the structure is 0.201. The structure confirms previously reported structures on the monomer level. However, the tetramer is much more densely packed. This adds a new level of complexity to the interpretation of mutational effects and challenges details in the current model for LacI function. Several amino acids, previously associated with changes in function but unexplained at the structural level, appear in a new structural context in this tetramer which provides new implications for their function. PubMed: 19004002DOI: 10.1002/prot.22284 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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