3TRW

Crystal structure of racemic villin headpiece subdomain crystallized in space group P-1

3TRW の概要

• エントリーDOI: 10.2210/pdb3trw/pdb
• 関連するPDBエントリー: 3TJW 3TRV 3TRY
• 分子名称: Villin-1 (2 entities in total)
• 機能のキーワード: racemate, quasi-racemate, d-amino acids, structural protein
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Cytoplasm, cytoskeleton: P02640
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 7947.24

構造登録者

Mortenson, D.E.,Satyshur, K.A.,Gellman, S.H.,Forest, K.T. (登録日: 2011-09-11, 公開日: 2012-01-25, 最終更新日: 2023-09-13)

主引用文献

Mortenson, D.E.,Satyshur, K.A.,Guzei, I.A.,Forest, K.T.,Gellman, S.H.
Quasiracemic crystallization as a tool to assess the accommodation of noncanonical residues in nativelike protein conformations.
J.Am.Chem.Soc., 134:2473-2476, 2012

PubMed Abstract: Quasiracemic crystallization has been used to obtain high-resolution structures of two variants of the villin headpiece subdomain (VHP) that contain a pentafluorophenylalanine (F(5)Phe) residue in the hydrophobic core. In each case, the crystal contained the variant constructed from l-amino acids and the native sequence constructed from d-amino acids. We were motivated to undertake these studies by reports that racemic proteins crystallize more readily than homochiral forms and the prospect that quasiracemic crystallization would enable us to determine whether a polypeptide containing a noncanonical residue can closely mimic the tertiary structure of the native sequence. The results suggest that quasiracemic crystallization may prove to be generally useful for assessing mimicry of naturally evolved protein folding patterns by polypeptides that contain unnatural side-chain or backbone subunits.

PubMed: 22280019
DOI: 10.1021/ja210045s

実験手法

X-RAY DIFFRACTION (2.1 Å)