1SYB

TRANSFER OF A BETA-TURN STRUCTURE TO A NEW PROTEIN CONTEXT

1SYB の概要

• エントリーDOI: 10.2210/pdb1syb/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: hydrolase(phosphoric diester)
• 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: 17240.45

構造登録者

Hynes, T.R.,Kautz, R.A.,Goodman, M.A.,Gill, J.F.,Fox, R.O. (登録日: 1994-01-07, 公開日: 1994-07-31, 最終更新日: 2024-02-14)

主引用文献

Hynes, T.R.,Kautz, R.A.,Goodman, M.A.,Gill, J.F.,Fox, R.O.
Transfer of a beta-turn structure to a new protein context.
Nature, 339:73-76, 1989

PubMed Abstract: Four-residue beta-turns and larger loop structures represent a significant fraction of globular protein surfaces and play an important role in determining the conformation and specificity of enzyme active sites and antibody-combining sites. Turns are an attractive starting point to develop protein design methods, as they involve a small number of consecutive residues, adopt a limited number of defined conformations and are minimally constrained by packing interactions with the remainder of the protein. The ability to substitute one beta-turn geometry for another will extend protein engineering beyond the redecoration of fixed backbone conformations to include local restructuring and the repositioning of surface side chains. To determine the feasibility and to examine the effect of such a structural modification on the fold and thermodynamic stability of a globular protein, we have substituted a five-residue turn sequence from concanavalin A for a type I' beta-turn in staphylococcal nuclease. The resulting hybrid protein is folded and has full nuclease enzymatic activity but reduced thermodynamic stability. The crystal structure of the hybrid protein reveals that the guest turn sequence retains the conformation of the parent concanavalin A structure when substituted in the nuclease host.

PubMed: 2716830
DOI: 10.1038/339073a0

実験手法

X-RAY DIFFRACTION (1.8 Å)