6K1O

Apo form of a putative cystathionine gamma-lyase

6K1O の概要

• エントリーDOI: 10.2210/pdb6k1o/pdb
• 分子名称: Cystathionine gamma-lyase (2 entities in total)
• 機能のキーワード: cse, cgl, biomineralization, quantum dots, cds, biosynthetic protein, lyase
• 由来する生物種: Stenotrophomonas maltophilia (strain R551-3)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 166810.20

構造登録者

Chen, S.,Wang, Y. (登録日: 2019-05-10, 公開日: 2020-05-13, 最終更新日: 2023-11-22)

主引用文献

Wang, Y.,Chen, H.,Huang, Z.,Yang, M.,Yu, H.,Peng, M.,Yang, Z.,Chen, S.
Structural characterization of cystathionine gamma-lyase smCSE enables aqueous metal quantum dot biosynthesis.
Int.J.Biol.Macromol., 174:42-51, 2021

PubMed Abstract: The development and utilization of inorganic material biosynthesis have evolved into single macromolecular systems. A putative cystathionine γ-lyase of bacteria Stenotrophomonas maltophilia (smCSE) is a newly identified biomolecule that enables the synthesis of nanomaterials. Due to the lack of structural information, the mechanism of smCSE biosynthesis remains unclear. Herein, we obtain two atomic-resolution smCSE-form X-ray structures and confirm that the conformational changes of Tyr108 and Lys206 within the enzyme active sites are critical for the protein-driven synthesis of metal sulfide quantum dots (QDs). The structural stability of tetramer and the specificity of surface amino acids are the basis for smCSE to synthesize quantum dots. The size of QD products can be regulated by predesigned amino acids and the morphology can be controlled through proteolytic treatments. The growth rate is enhanced by the stabilization of a flexible loop in the active site, as shown by the X-ray structure of the engineered protein which fused with a dodecapeptide. We further prove that the smCSE-driven route can be applied to the general synthesis of other metal sulfide nanoparticles. These results provide a better understanding of the mechanism of QD biosynthesis and a new perspective on the control of this biosynthesis by protein modification.

PubMed: 33497694
DOI: 10.1016/j.ijbiomac.2021.01.141

実験手法

X-RAY DIFFRACTION (2.033 Å)