4EFG

Crystal Structure of the Q108K:K40L:T51V:T53C:Y19W:R58W:T29L Mutant of Cellular Retinol Binding Protein Type II in Complex with All-trans-Retinal at 1.58 Angstrom Resolution

4EFG の概要

• エントリーDOI: 10.2210/pdb4efg/pdb
• 関連するPDBエントリー: 4EDE 4EEJ
• 分子名称: Retinol-binding protein 2, RETINAL, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: retinal complex, beta barrel, transport protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P50120
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31980.27

構造登録者

Nossoni, Z.,Geiger, J.H. (登録日: 2012-03-29, 公開日: 2012-12-26, 最終更新日: 2024-10-16)

主引用文献

Wang, W.,Nossoni, Z.,Berbasova, T.,Watson, C.T.,Yapici, I.,Lee, K.S.,Vasileiou, C.,Geiger, J.H.,Borhan, B.
Tuning the electronic absorption of protein-embedded all-trans-retinal.
Science, 338:1340-1343, 2012

PubMed Abstract: Protein-chromophore interactions are a central component of a wide variety of critical biological processes such as color vision and photosynthesis. To understand the fundamental elements that contribute to spectral tuning of a chromophore inside the protein cavity, we redesigned human cellular retinol binding protein II (hCRBPII) to fully encapsulate all-trans-retinal and form a covalent bond as a protonated Schiff base. This system, using rational mutagenesis designed to alter the electrostatic environment within the binding pocket of the host protein, enabled regulation of the absorption maximum of the pigment in the range of 425 to 644 nanometers. With only nine point mutations, the hCRBPII mutants induced a systematic shift in the absorption profile of all-trans-retinal of more than 200 nanometers across the visible spectrum.

PubMed: 23224553
DOI: 10.1126/science.1226135

実験手法

X-RAY DIFFRACTION (1.58 Å)