2WV1

CRYSTAL STRUCTURE OF THE HLYIIR MUTANT PROTEIN WITH RESIDUES 169-186 SUBSTITUTED BY A LINKER CONTAINING TWO THROMBIN SITES

2WV1 の概要

• エントリーDOI: 10.2210/pdb2wv1/pdb
• 関連するPDBエントリー: 2FX0 2JJ7 2JK3
• 分子名称: HEMOLYSIN II REGULATORY PROTEIN, NITRATE ION (3 entities in total)
• 機能のキーワード: transcription, transcription regulation, tetr family
• 由来する生物種: BACILLUS CEREUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 46154.87

構造登録者

Kovalevskiy, O.V.,Solonin, A.S.,Antson, A.A. (登録日: 2009-10-12, 公開日: 2009-10-20, 最終更新日: 2023-12-20)

主引用文献

Kovalevskiy, O.V.,Solonin, A.S.,Antson, A.A.
Structural Investigation of Transcriptional Regulator Hlyiir: Influence of a Disordered Region on Protein Fold and Dimerization.
Proteins, 78:1870-, 2010

PubMed Abstract: B. cereus HlyIIR belongs to the TetR family of dimeric transcriptional regulators. Unlike other members of the TetR family, HlyIIR contains an insert between alpha-helices alpha8 and alpha9, which is located at the subunit-subunit interface. N-terminal segment of this insert (amino acids, Pro161-Ser169) forms a short alpha-helix alpha8* that occupies a complementary cavity on the surface of the adjacent subunit, whereas the C-terminal segment comprising 16 amino acids (Leu170-Glu185) is disordered. To understand whether this disordered segment is important for protein's function, we determined crystal structures of two engineered HlyIIR proteins where this segment was either substituted by a seven-residue flexible Ser-Gly linker or replaced by a cleavable peptide containing proteolytic sites at both ends. Unexpectedly, alteration or proteolytic removal of the disordered segment resulted in changes in protein's conformation and in a remarkable rearrangement at the subunit-subunit interface. X-ray structures of the two engineered proteins revealed an unusual plasticity at the dimerization interface of HlyIIR enabling it to form dimers stabilized by different sets of interactions. Structural comparison indicates that in spite of the flexible nature of the disordered segment, it is critical for maintaining the native structure as it influences the position of alpha8*. The data demonstrate how disordered loops on protein surfaces may affect folding and subunit-subunit interactions.

PubMed: 20225260
DOI: 10.1002/PROT.22700

実験手法

X-RAY DIFFRACTION (2.3 Å)