4HXT

Crystal Structure of Engineered Protein. Northeast Structural Genomics Consortium Target OR329

4HXT の概要

• エントリーDOI: 10.2210/pdb4hxt/pdb
• 分子名称: De Novo Protein OR329 (2 entities in total)
• 機能のキーワード: structural genomics, psi-biology, protein structure initiative, northeast structural genomics consortium, nesg, de novo protein
• 由来する生物種: artificial gene
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26073.20

構造登録者

Vorobiev, S.,Su, M.,Parmeggiani, F.,Seetharaman, J.,Huang, P.-S.,Maglaqui, M.,Xiao, X.,Lee, D.,Everett, J.K.,Acton, T.B.,Baker, D.,Montelione, G.T.,Tong, L.,Hunt, J.F.,Northeast Structural Genomics Consortium (NESG) (登録日: 2012-11-12, 公開日: 2012-11-21, 最終更新日: 2024-10-30)

主引用文献

Fallas, J.A.,Ueda, G.,Sheffler, W.,Nguyen, V.,McNamara, D.E.,Sankaran, B.,Pereira, J.H.,Parmeggiani, F.,Brunette, T.J.,Cascio, D.,Yeates, T.R.,Zwart, P.,Baker, D.
Computational design of self-assembling cyclic protein homo-oligomers.
NAT.CHEM., 9:353-360, 2017

PubMed Abstract: Self-assembling cyclic protein homo-oligomers play important roles in biology, and the ability to generate custom homo-oligomeric structures could enable new approaches to probe biological function. Here we report a general approach to design cyclic homo-oligomers that employs a new residue-pair-transform method to assess the designability of a protein-protein interface. This method is sufficiently rapid to enable the systematic enumeration of cyclically docked arrangements of a monomer followed by sequence design of the newly formed interfaces. We use this method to design interfaces onto idealized repeat proteins that direct their assembly into complexes that possess cyclic symmetry. Of 96 designs that were characterized experimentally, 21 were found to form stable monodisperse homo-oligomers in solution, and 15 (four homodimers, six homotrimers, six homotetramers and one homopentamer) had solution small-angle X-ray scattering data consistent with the design models. X-ray crystal structures were obtained for five of the designs and each is very close to their corresponding computational model.

PubMed: 28338692
DOI: 10.1038/nchem.2673

実験手法

X-RAY DIFFRACTION (1.95 Å)