Folding of S6 structures with divergent amino acid composition: Pathway flexibility within partly overlapping foldons
Olofsson, Maria ; Hansson, Sebastian LU ; Hedberg, Linda ; Logan, Derek LU
and Oliveberg, Mikael
(2007)
In Journal of Molecular Biology
365(1).
p.237-248
- Abstract
- Studies of circular permutants have demonstrated that the folding reaction of S6 from Thermus thermophilus (S6(T)) is malleable and responds in an ordered manner to changes of the sequence separation between interacting residues: the S6(T) permutants retain a common nucleation pattern in the form of a two-strand-helix motif that can be recruited from different parts of the structure. To further test the robustness of the two-strand-helix nucleus we have here determined the crystal structure and folding reaction of an evolutionary divergent S6 protein from the hyperthermophilic bacterium Aquifex aeolicus (S6(A)). Although the overall topology of S6(A) is very similar to that of S6(T) the architecture of the hydrophobic core is radically... (More)
- Studies of circular permutants have demonstrated that the folding reaction of S6 from Thermus thermophilus (S6(T)) is malleable and responds in an ordered manner to changes of the sequence separation between interacting residues: the S6(T) permutants retain a common nucleation pattern in the form of a two-strand-helix motif that can be recruited from different parts of the structure. To further test the robustness of the two-strand-helix nucleus we have here determined the crystal structure and folding reaction of an evolutionary divergent S6 protein from the hyperthermophilic bacterium Aquifex aeolicus (S6(A)). Although the overall topology of S6(A) is very similar to that of S6(T) the architecture of the hydrophobic core is radically different by containing a large proportion of stacked Phe side-chains. Despite this disparate core composition, the folding rate constant and the kinetic m values of S6(A) are identical to those of S6(T). The folding nucleus of S6(A) is also found to retain the characteristic two-strand-helix motif of the S6(T) permutants, but with a new structural emphasis. The results suggest that the protein folding reaction is linked to topology only in the sense that the native-state topology determines the repertoire of accessible nucleation motifs. If the native structure allows several equivalent ways of recruiting a productive nucleus the folding reaction is free to redistribute within these topological constraints. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/680073
- author
- Olofsson, Maria
; Hansson, Sebastian
LU
; Hedberg, Linda
; Logan, Derek
LU
and Oliveberg, Mikael
- organization
- publishing date
- 2007
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- thermophile, folding energy landscape, folding nucleus, transition state, foldons
- in
- Journal of Molecular Biology
- volume
- 365
- issue
- 1
- pages
- 237 - 248
- publisher
- Elsevier
- external identifiers
-
- wos:000243199300020
- scopus:33751411136
- ISSN
- 1089-8638
- DOI
- 10.1016/j.jmb.2006.09.016
- language
- English
- LU publication?
- yes
- id
- 1a3ca0b6-8036-4257-a172-e3fc6ed86baf (old id 680073)
- date added to LUP
- 2016-04-01 15:57:13
- date last changed
- 2022-04-07 01:55:31
@article{1a3ca0b6-8036-4257-a172-e3fc6ed86baf,
abstract = {{Studies of circular permutants have demonstrated that the folding reaction of S6 from Thermus thermophilus (S6(T)) is malleable and responds in an ordered manner to changes of the sequence separation between interacting residues: the S6(T) permutants retain a common nucleation pattern in the form of a two-strand-helix motif that can be recruited from different parts of the structure. To further test the robustness of the two-strand-helix nucleus we have here determined the crystal structure and folding reaction of an evolutionary divergent S6 protein from the hyperthermophilic bacterium Aquifex aeolicus (S6(A)). Although the overall topology of S6(A) is very similar to that of S6(T) the architecture of the hydrophobic core is radically different by containing a large proportion of stacked Phe side-chains. Despite this disparate core composition, the folding rate constant and the kinetic m values of S6(A) are identical to those of S6(T). The folding nucleus of S6(A) is also found to retain the characteristic two-strand-helix motif of the S6(T) permutants, but with a new structural emphasis. The results suggest that the protein folding reaction is linked to topology only in the sense that the native-state topology determines the repertoire of accessible nucleation motifs. If the native structure allows several equivalent ways of recruiting a productive nucleus the folding reaction is free to redistribute within these topological constraints.}},
author = {{Olofsson, Maria and Hansson, Sebastian and Hedberg, Linda and Logan, Derek and Oliveberg, Mikael}},
issn = {{1089-8638}},
keywords = {{thermophile; folding energy landscape; folding nucleus; transition state; foldons}},
language = {{eng}},
number = {{1}},
pages = {{237--248}},
publisher = {{Elsevier}},
series = {{Journal of Molecular Biology}},
title = {{Folding of S6 structures with divergent amino acid composition: Pathway flexibility within partly overlapping foldons}},
url = {{http://dx.doi.org/10.1016/j.jmb.2006.09.016}},
doi = {{10.1016/j.jmb.2006.09.016}},
volume = {{365}},
year = {{2007}},
}