1QX8

Crystal structure of a five-residue deletion mutant of the Rop protein

1QX8 の概要

• エントリーDOI: 10.2210/pdb1qx8/pdb
• 関連するPDBエントリー: 1B6Q 1GMG 1ROP 1RPO
• 分子名称: Regulatory protein ROP (2 entities in total)
• 機能のキーワード: replication; initiation of transcription; rna primer; x-ray, transcription
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13357.09

構造登録者

Glykos, N.M.,Vlassi, M.,Papanikolaou, Y.,Kotsifaki, D.,Cesareni, G.,Kokkinidis, M. (登録日: 2003-09-04, 公開日: 2004-09-28, 最終更新日: 2023-08-23)

主引用文献

Glykos, N.M.,Papanikolau, Y.,Vlassi, M.,Kotsifaki, D.,Cesareni, G.,Kokkinidis, M.
Loopless Rop: structure and dynamics of an engineered homotetrameric variant of the repressor of primer protein.
Biochemistry, 45:10905-10919, 2006

PubMed Abstract: The repressor of primer (Rop) protein has become a steady source of surprises concerning the relationship between the sequences and the structures of several of its mutants and variants. Here we add another piece to the puzzle of Rop by showing that an engineered deletion mutant of the protein (corresponding to a deletion of residues 30-34 of the wild-type protein and designed to restore the heptad periodicity at the turn region) results in a complete reorganization of the bundle which is converted from a homodimer to a homotetramer. In contrast (and as previously shown), a two-residue insertion, which also restores the heptad periodicity, is essentially identical with wild-type Rop. The new deletion mutant structure is a canonical, left-handed, all-antiparallel bundle with a completely different hydrophobic core and distinct surface properties. The structure agrees and qualitatively explains the results from functional, thermodynamic, and kinetic studies which indicated that this deletion mutant is a biologically inactive hyperstable homotetramer. Additional insight into the stability and dynamics of the mutant structure has been obtained from extensive molecular dynamics simulations in explicit water and with full treatment of electrostatics.

PubMed: 16953576
DOI: 10.1021/bi060833n

実験手法

X-RAY DIFFRACTION (2.02 Å)