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:
https://lup.lub.lu.se/record/3635003
- author
- Stenberg, Kaj A E
and Vihinen, Mauno
LU
- publishing date
- 2009
- 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 Inc.
- external identifiers
-
- pmid:19004002
- scopus:66149124113
- pmid:19004002
- 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
- 2016-04-04 09:04:10
- date last changed
- 2022-02-20 23:01:00
@article{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}},
keywords = {{Computational Biology: methods; Escherichia coli: chemistry; Escherichia coli Proteins: chemistry; Glycols: chemistry; Repressor Proteins: chemistry}},
language = {{eng}},
number = {{3}},
pages = {{748--759}},
publisher = {{John Wiley & Sons Inc.}},
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}},
doi = {{10.1002/prot.22284}},
volume = {{75}},
year = {{2009}},
}