3CWO

A beta/alpha-barrel built by the combination of fragments from different folds

3CWO の概要

• エントリーDOI: 10.2210/pdb3cwo/pdb
• 関連するPDBエントリー: 1THF 1TMY
• 分子名称: beta/alpha-barrel protein based on 1THF and 1TMY, SULFATE ION (3 entities in total)
• 機能のキーワード: xray, chey, hisf, half barrel, de novo protein
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26144.26

構造登録者

Bharat, T.A.M.,Eisenbeis, S.,Zeth, K.,Hocker, B. (登録日: 2008-04-22, 公開日: 2008-07-08, 最終更新日: 2023-08-30)

主引用文献

Bharat, T.A.,Eisenbeis, S.,Zeth, K.,Hocker, B.
A beta alpha-barrel built by the combination of fragments from different folds.
Proc.Natl.Acad.Sci.Usa, 105:9942-9947, 2008

PubMed Abstract: Combinatorial assembly of protein domains plays an important role in the evolution of proteins. There is also evidence that protein domains have come together from stable subdomains. This concept of modular assembly could be used to construct new well folded proteins from stable protein fragments. Here, we report the construction of a chimeric protein from parts of a (betaalpha)(8)-barrel enzyme from histidine biosynthesis pathway (HisF) and a protein of the (betaalpha)(5)-flavodoxin-like fold (CheY) from Thermotoga maritima that share a high structural similarity. We expected this construct to fold into a full (betaalpha)(8)-barrel. Our results show that the chimeric protein is a stable monomer that unfolds with high cooperativity. Its three-dimensional structure, which was solved to 3.1 A resolution by x-ray crystallography, confirms a barrel-like fold in which the overall structures of the parent proteins are highly conserved. The structure further reveals a ninth strand in the barrel, which is formed by residues from the HisF C terminus and an attached tag. This strand invades between beta-strand 1 and 2 of the CheY part closing a gap in the structure that might be due to a suboptimal fit between the fragments. Thus, by a combination of parts from two different folds and a small arbitrary fragment, we created a well folded and stable protein.

PubMed: 18632584
DOI: 10.1073/pnas.0802202105

実験手法

X-RAY DIFFRACTION (3.1 Å)