Structural highlights
Function
[LACI_ECOLI] Repressor of the lactose operon. Binds allolactose as an inducer.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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. Proteins 2009. (c) 2008 Wiley-Liss, Inc.
Crystal structure of a 1.6-hexanediol bound tetrameric form of Escherichia coli Lac-repressor refined to 2.1 A resolution.,Stenberg KA, Vihinen M Proteins. 2008 Sep 30. PMID:19004002[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Stenberg KA, Vihinen M. Crystal structure of a 1.6-hexanediol bound tetrameric form of Escherichia coli Lac-repressor refined to 2.1 A resolution. Proteins. 2008 Sep 30. PMID:19004002 doi:10.1002/prot.22284
