Crystal structure of a 1.6-hexanediol bound tetrameric form of Escherichia coli lac-repressor refined to 2.1 A resolution.
Författare
Summary, in English
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.
Publiceringsår
2009
Språk
Engelska
Sidor
748-759
Publikation/Tidskrift/Serie
Proteins
Volym
75
Issue
3
Länkar
Dokumenttyp
Artikel i tidskrift
Förlag
John Wiley & Sons Inc.
Ämne
- Medical Genetics
Nyckelord
- Computational Biology: methods
- Escherichia coli: chemistry
- Escherichia coli Proteins: chemistry
- Glycols: chemistry
- Repressor Proteins: chemistry
Status
Published
ISBN/ISSN/Övrigt
- ISSN: 0887-3585