8Q52

A PBP-like protein built from fragments of different folds

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8Q52 の概要

• エントリーDOI: 10.2210/pdb8q52/pdb
• 分子名称: Leucine-specific-binding protein,Chemotaxis protein CheY, SULFATE ION (3 entities in total)
• 機能のキーワード: protein fold evolution, gene duplication, flavodoxin-like fold, periplasmic-binding protein-like i fold, sub-domain, chimeric proteins, homology, de novo protein
• 由来する生物種: Escherichia coli K-12; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34842.78

構造登録者

Shanmugaratnam, S.,Toledo-Patino, S.,Goetz, S.K.,Farias-Rico, J.A.,Hocker, B. (登録日: 2023-08-08, 公開日: 2024-04-10, 最終更新日: 2024-11-20)

主引用文献

Toledo-Patino, S.,Goetz, S.K.,Shanmugaratnam, S.,Hocker, B.,Farias-Rico, J.A.
Molecular handcraft of a well-folded protein chimera.
Febs Lett., 598:1375-1386, 2024

PubMed Abstract: Modular assembly is a compelling pathway to create new proteins, a concept supported by protein engineering and millennia of evolution. Natural evolution provided a repository of building blocks, known as domains, which trace back to even shorter segments that underwent numerous 'copy-paste' processes culminating in the scaffolds we see today. Utilizing the subdomain-database Fuzzle, we constructed a fold-chimera by integrating a flavodoxin-like fragment into a periplasmic binding protein. This chimera is well-folded and a crystal structure reveals stable interfaces between the fragments. These findings demonstrate the adaptability of α/β-proteins and offer a stepping stone for optimization. By emphasizing the practicality of fragment databases, our work pioneers new pathways in protein engineering. Ultimately, the results substantiate the conjecture that periplasmic binding proteins originated from a flavodoxin-like ancestor.

PubMed: 38508768
DOI: 10.1002/1873-3468.14856

実験手法

X-RAY DIFFRACTION (2.15 Å)