3A2G
Crystal Structure of K102C-Myoglobin conjugated with Fluorescein
Summary for 3A2G
| Entry DOI | 10.2210/pdb3a2g/pdb |
| Descriptor | Myoglobin, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (6 entities in total) |
| Functional Keywords | oxygen storage/transport, oxygen transport, heme, iron, metal-binding, muscle protein, transport |
| Biological source | Physeter catodon (Sperm whale) |
| Total number of polymer chains | 1 |
| Total formula weight | 18450.00 |
| Authors | Koshiyama, T.,Hikage, T.,Ueno, T. (deposition date: 2009-05-20, release date: 2010-03-02, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 20099839DOI: 10.1021/bc9003052 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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