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Crystal structure of a 1.6-hexanediol bound tetrameric form of Escherichia coli lac-repressor refined to 2.1 A resolution.

Stenberg, Kaj A E and Vihinen, Mauno LU (2009) In Proteins 75(3). p.748-759
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... (More)
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. (Less)
Please use this url to cite or link to this publication:
author
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Computational Biology: methods, Escherichia coli: chemistry, Escherichia coli Proteins: chemistry, Glycols: chemistry, Repressor Proteins: chemistry
in
Proteins
volume
75
issue
3
pages
748 - 759
publisher
John Wiley & Sons
external identifiers
  • PMID:19004002
  • Scopus:66149124113
ISSN
0887-3585
DOI
10.1002/prot.22284
language
English
LU publication?
no
id
b9701827-0915-488d-982b-5fcc0194f808 (old id 3635003)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/19004002?dopt=Abstract
date added to LUP
2013-06-12 16:32:41
date last changed
2016-10-13 04:23:19
@misc{b9701827-0915-488d-982b-5fcc0194f808,
  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.},
  author       = {Stenberg, Kaj A E and Vihinen, Mauno},
  issn         = {0887-3585},
  keyword      = {Computational Biology: methods,Escherichia coli: chemistry,Escherichia coli Proteins: chemistry,Glycols: chemistry,Repressor Proteins: chemistry},
  language     = {eng},
  number       = {3},
  pages        = {748--759},
  publisher    = {ARRAY(0x82e65d8)},
  series       = {Proteins},
  title        = {Crystal structure of a 1.6-hexanediol bound tetrameric form of Escherichia coli lac-repressor refined to 2.1 A resolution.},
  url          = {http://dx.doi.org/10.1002/prot.22284},
  volume       = {75},
  year         = {2009},
}