3A2G

Crystal Structure of K102C-Myoglobin conjugated with Fluorescein

3A2G の概要

• エントリーDOI: 10.2210/pdb3a2g/pdb
• 分子名称: Myoglobin, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: oxygen storage/transport, oxygen transport, heme, iron, metal-binding, muscle protein, transport
• 由来する生物種: Physeter catodon (Sperm whale)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18450.00

構造登録者

Koshiyama, T.,Hikage, T.,Ueno, T. (登録日: 2009-05-20, 公開日: 2010-03-02, 最終更新日: 2024-10-30)

主引用文献

Koshiyama, T.,Kawaba, N.,Hikage, T.,Shirai, M.,Miura, Y.,Huang, C.-Y.,Tanaka, K.,Watanabe, Y.,Ueno, T.
Modification of porous protein crystals in development of biohybrid materials
Bioconjug.Chem., 21:264-269, 2010

PubMed Abstract: Protein assemblies have attracted increasing attention for construction of biohybrid materials. Protein crystals can also be regarded as solid protein assemblies. The present work demonstrates that protein crystals can be employed as porous biomaterials by site-specific modifications of the crystals of recombinant sperm whale myoglobin mutants. The myoglobin crystals of space group P6 provide hexagonal pores consisting of the building blocks of six Mb molecules, which form a pore with a diameter of 40 A. On the basis of the lattice structure of the Mb crystals, we have selected appropriate residues located on the surface of the pores for replacement with cysteine. This enables modification of the pore surface via coupling with maleimide derivatives. We have succeeded in crystallizing the modified Mb mutants, retaining the P6 lattice, and consistently aligning nanosized functional molecules such as fluorescein, eosin, and Ru(bpy)(3) into the hexagonal pores of the Mb crystals. Our strategy for site-specific modification of protein crystal pores is applicable to various protein crystals with porous structures. We believe that modified porous protein crystals will provide attractive candidates for novel solid materials in nanotechnology applications.

PubMed: 20099839
DOI: 10.1021/bc9003052

実験手法

X-RAY DIFFRACTION (1.75 Å)