1EM7

HELIX VARIANT OF THE B1 DOMAIN FROM STREPTOCOCCAL PROTEIN G

1EM7 の概要

• エントリーDOI: 10.2210/pdb1em7/pdb
• 関連するPDBエントリー: 1gb4 1pga
• 分子名称: PROTEIN G (2 entities in total)
• 機能のキーワード: helix propensity, helix dipole interaction, protein design, protein g, membrane protein
• 由来する生物種: Streptococcus sp.
• 細胞内の位置: Secreted, cell wall ; Peptidoglycan-anchor : P06654
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6287.90

構造登録者

Strop, P.,Marinescu, A.M.,Mayo, S.L. (登録日: 2000-03-16, 公開日: 2002-05-08, 最終更新日: 2024-02-07)

主引用文献

Strop, P.,Marinescu, A.M.,Mayo, S.L.
Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design.
Protein Sci., 9:1391-1394, 2000

PubMed Abstract: Six helix surface positions of protein G (Gbeta1) were redesigned using a computational protein design algorithm, resulting in the five fold mutant Gbeta1m2. Gbeta1m2 is well folded with a circular dichroism spectrum nearly identical to that of Gbeta1, and a melting temperature of 91 degrees C, approximately 6 degrees C higher than that of Gbeta1. The crystal structure of Gbeta1m2 was solved to 2.0 A resolution by molecular replacement. The absence of hydrogen bond or salt bridge interactions between the designed residues in Gbeta1m2 suggests that the increased stability of Gbeta1m2 is due to increased helix propensity and more favorable helix dipole interactions.

PubMed: 10933505

実験手法

X-RAY DIFFRACTION (2 Å)