2J5A

Folding of S6 structures with divergent amino-acid composition: pathway flexibility within partly overlapping foldons

2J5A の概要

• エントリーDOI: 10.2210/pdb2j5a/pdb
• 分子名称: 30S RIBOSOMAL PROTEIN S6, SODIUM ION (3 entities in total)
• 機能のキーワード: aquifex aeolicus, ribosomal protein, ribonucleoprotein, ribosomal protein s6, rna-binding, rrna-binding, protein folding
• 由来する生物種: AQUIFEX AEOLICUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13482.43

構造登録者

Hansson, S.,Olofsson, L.,Hedberg, L.,Oliveberg, M.,Logan, D.T. (登録日: 2006-09-13, 公開日: 2006-10-25, 最終更新日: 2023-12-13)

主引用文献

Olofsson, M.,Hansson, S.,Hedberg, L.,Logan, D.T.,Oliveberg, M.
Folding of S6 Structures with Divergent Amino Acid Composition: Pathway Flexibility within Partly Overlapping Foldons.
J.Mol.Biol., 365:237-, 2007

PubMed 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.

PubMed: 17056063
DOI: 10.1016/J.JMB.2006.09.016

実験手法

X-RAY DIFFRACTION (2.3 Å)