금주의 세미나

[BK21 SEMINAR] Dr. Tae Su Choi (University of California, San Diego)_2…

페이지 정보

댓글 0건 조회 650회 작성일 22-01-03 11:13

본문

♧Title: Design of metal-selective protein using flexible dimer-interface

♧ Speaker :  Dr. Tae Su Choi (University of California, San Diego)

♧ Date : 2022. 1. 6 (THU), 16:00 PM

♧URL: https://us02web.zoom.us/j/88601997658?pwd=T1BTdzIvZm1QcEcyL1pXNVh4WUFrdz09

 

 

Design of metal-selective protein using flexible dimer-interface

 

Metalloproteins are closely associated with vital functions of living organisms such as metal homeostasis and enzymatic reactions. Central to the functions of metalloproteins is selective metal coordination: each metalloprotein must pair with its cognate metallocofactor to fulfill its biological role. Cells regulate selective incorporation of biologically essential, first row mid-to-late transition metal ions using metallochaperones and metal sensor proteins. Without the aid of the intracellular regulatory mechanisms, most of the metalloproteins in heterogeneous environment exhibits low fidelity in metal selectivity. Inherently flexible motions of protein backbones and side chains disrupt steric selection of the metal ions whose d-orbital electron configurations determine preferred coordination geometries. Accordingly, a large number of metalloproteins have been reported to generally follow Irving-Williams (IW) series (MnII < FeII < CoII < NiII < CuII > ZnII) in binding affinities between the metal ions and the proteins, thereby losing their intrinsic structural/catalytic functionalities.
Here, I will introduce a design strategy of artificial dimeric proteins that thermodynamically overcome the IW restrictions in vitro and in bacterial cells, favoring binding of lower-IW transition metals over CuII – the most dominant ion in the IW series. The dimeric proteins were designed to be flexible through single disulfide bond. The flexibility of the dimer interface adopts mutually exclusive, metal-dependent conformational states with structural cooperativity between multiple metal binding sites. Consequently, the binding sites of metal ions (CoII, NiII, and ZnII) thermodynamically disfavor CuII ions by enforcing an unfavorable coordination geometry. This approach demonstrates that the flexible interface would be significant as a new design element for constructing artificial metalloproteins with new-to-nature functions.

 

 

 

Host : Prof. Jongcheol Seo (T.279-2341)

댓글목록

등록된 댓글이 없습니다.