1A2U

STAPHYLOCOCCAL NUCLEASE, V23C VARIANT, COMPLEX WITH 1-N-BUTANE THIOL AND 3',5'-THYMIDINE DIPHOSPHATE

1A2U の概要

• エントリーDOI: 10.2210/pdb1a2u/pdb
• 分子名称: STAPHYLOCOCCAL NUCLEASE, CALCIUM ION, THYMIDINE-3',5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: nuclease, unnatural amino acid, hydrolase, endonuclease
• 由来する生物種: Staphylococcus aureus
• 細胞内の位置: Nuclease A: Secreted. Nuclease B: Membrane: P00644
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17377.78

構造登録者

Wynn, R.,Harkins, P.C.,Richards, F.M.,Fox, R.O. (登録日: 1998-01-11, 公開日: 1998-04-29, 最終更新日: 2023-08-02)

主引用文献

Wynn, R.,Harkins, P.C.,Richards, F.M.,Fox, R.O.
Mobile unnatural amino acid side chains in the core of staphylococcal nuclease.
Protein Sci., 5:1026-1031, 1996

PubMed Abstract: The structures of several variants of staphylococcal nuclease with long flexible unnatural amino acid side chains in the hydrophobic core have been determined by X-ray crystallography. The unnatural amino acids are disulfide moieties between the lone cysteine residue in V23C nuclease and methane, ethane, 1-n-propane, 1-n-butane, 1-n-pentane, and 2-hydroxyethyl thiols. We have examined changes in the core packing of these mutants. Side chains as large as the 1-n-propyl cysteine disulfide can be incorporated without perturbation of the structure. This is due, in part, to cavities present in the wild-type protein. The longest side chains are not well defined, even though they remain buried within the protein interior. These results suggest that the enthalpy-entropy balance that governs the rigidity of protein interiors favors tight packing only weakly. Additionally, the tight packing observed normally in protein interiors may reflect, in part, the limited numbers of rotamers available to the natural amino acids.

PubMed: 8762134

実験手法

X-RAY DIFFRACTION (2 Å)