4XC7

Isobutyryl-CoA mutase fused with bound butyryl-CoA and without cobalamin or GDP (apo-IcmF)

4XC7 の概要

• エントリーDOI: 10.2210/pdb4xc7/pdb
• 関連するPDBエントリー: 4XC6 4XC8
• 分子名称: Isobutyryl-CoA mutase fused, Butyryl Coenzyme A, L(+)-TARTARIC ACID (3 entities in total)
• 機能のキーワード: radical enzyme, complex, isomerase, g-protein chaperone
• 由来する生物種: Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 247830.59

構造登録者

Jost, M.,Drennan, C.L. (登録日: 2014-12-17, 公開日: 2015-02-11, 最終更新日: 2023-09-27)

主引用文献

Jost, M.,Cracan, V.,Hubbard, P.A.,Banerjee, R.,Drennan, C.L.
Visualization of a radical B12 enzyme with its G-protein chaperone.
Proc.Natl.Acad.Sci.USA, 112:2419-2424, 2015

PubMed Abstract: G-protein metallochaperones ensure fidelity during cofactor assembly for a variety of metalloproteins, including adenosylcobalamin (AdoCbl)-dependent methylmalonyl-CoA mutase and hydrogenase, and thus have both medical and biofuel development applications. Here, we present crystal structures of IcmF, a natural fusion protein of AdoCbl-dependent isobutyryl-CoA mutase and its corresponding G-protein chaperone, which reveal the molecular architecture of a G-protein metallochaperone in complex with its target protein. These structures show that conserved G-protein elements become ordered upon target protein association, creating the molecular pathways that both sense and report on the cofactor loading state. Structures determined of both apo- and holo-forms of IcmF depict both open and closed enzyme states, in which the cofactor-binding domain is alternatively positioned for cofactor loading and for catalysis. Notably, the G protein moves as a unit with the cofactor-binding domain, providing a visualization of how a chaperone assists in the sequestering of a precious cofactor inside an enzyme active site.

PubMed: 25675500
DOI: 10.1073/pnas.1419582112

実験手法

X-RAY DIFFRACTION (3.45 Å)