5LYC

Cytochrome c in complex with phosphonato-calix[6]arene

5LYC の概要

• エントリーDOI: 10.2210/pdb5lyc/pdb
• 分子名称: Cytochrome c iso-1, HEME C, phosphonato-calix[6]arene, ... (5 entities in total)
• 機能のキーワード: calixarene, dimer, surface-binding, oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28034.08

構造登録者

Rennie, M.L.,Crowley, P.B. (登録日: 2016-09-27, 公開日: 2017-05-10, 最終更新日: 2024-11-13)

主引用文献

Rennie, M.L.,Doolan, A.M.,Raston, C.L.,Crowley, P.B.
Protein Dimerization on a Phosphonated Calix[6]arene Disc.
Angew. Chem. Int. Ed. Engl., 56:5517-5521, 2017

PubMed Abstract: Complex formation between cationic cytochrome c and the water-soluble, poly-anionic p-phosphonatocalix[6]arene (pclx ) was investigated. A crystal structure (at 1.8 Å resolution) revealed a remarkable dimeric disc of pclx that acts like glue to mediate a symmetric (C ) protein dimer. The calixarene disc has a diameter of about 1.5 nm and masks about 360 Å of protein surface. The key protein-calixarene contacts occur via two linchpin lysines, with additional contacts provided by a small hydrophobic patch. The protein-calixarene supramolecular assemblies were observed in solution by size-exclusion chromatography with multi-angle light scattering and NMR spectroscopy. Using isothermal titration calorimetry and NMR data, an apparent K in the low micromolar range was determined for the charge-rich protein-calixarene complex. In contrast to p-sulfonatocalix[4]arene, the larger pclx has a single, well-defined binding site that mediates the assembly of cytochrome c in solution.

PubMed: 28407337
DOI: 10.1002/anie.201701500

実験手法

X-RAY DIFFRACTION (1.8 Å)