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4DO2

Crystal Structure of the Rop protein mutant D30P/A31G at resolution 1.4 resolution.

4DO2 の概要
エントリーDOI10.2210/pdb4do2/pdb
関連するPDBエントリー1ROP
分子名称Regulatory protein rop (2 entities in total)
機能のキーワードprotein structure, protein folding, rop protein, bacterial protein, mutation, 4-alpha-helical bundle, loop, rna binding protein, cole1 plasmid copy number
由来する生物種Escherichia coli
タンパク質・核酸の鎖数2
化学式量合計16326.07
構造登録者
Amprazi, M.,Kapetaniou, E.G.,Kokkinidis, M. (登録日: 2012-02-09, 公開日: 2013-02-13, 最終更新日: 2023-09-13)
主引用文献Amprazi, M.,Kotsifaki, D.,Providaki, M.,Kapetaniou, E.G.,Fellas, G.,Kyriazidis, I.,Perez, J.,Kokkinidis, M.
Structural plasticity of 4-alpha-helical bundles exemplified by the puzzle-like molecular assembly of the Rop protein.
Proc.Natl.Acad.Sci.USA, 111:11049-11054, 2014
Cited by
PubMed Abstract: The dimeric Repressor of Primer (Rop) protein, a widely used model system for the study of coiled-coil 4-α-helical bundles, is characterized by a remarkable structural plasticity. Loop region mutations lead to a wide range of topologies, folding states, and altered physicochemical properties. A protein-folding study of Rop and several loop variants has identified specific residues and sequences that are linked to the observed structural plasticity. Apart from the native state, native-like and molten-globule states have been identified; these states are sensitive to reducing agents due to the formation of nonnative disulfide bridges. Pro residues in the loop are critical for the establishment of new topologies and molten globule states; their effects, however, can be in part compensated by Gly residues. The extreme plasticity in the assembly of 4-α-helical bundles reflects the capacity of the Rop sequence to combine a specific set of hydrophobic residues into strikingly different hydrophobic cores. These cores include highly hydrated ones that are consistent with the formation of interchain, nonnative disulfide bridges and the establishment of molten globules. Potential applications of this structural plasticity are among others in the engineering of bio-inspired materials.
PubMed: 25024213
DOI: 10.1073/pnas.1322065111
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.401 Å)
構造検証レポート
Validation report summary of 4do2
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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