The effect of the adaptor protein Isd11 on the quaternary structure of the eukaryotic cysteine desulphurase Nfs1 |
| |
| Authors: | Kerem Teral? Rebecca L Beavil Richard W Pickersgill Mark van der Giezen |
| |
| Institution: | 1. School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London E1 4NS, UK;2. Randall Division of Cell and Molecular Biophysics, King’s College London, New Hunt’s House, Guy’s Campus, London SE1 1UL, UK;3. Biocatalysis Centre, Biosciences, College of Life & Environmental Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, UK |
| |
| Abstract: | Small inorganic assemblies of alternating ferrous/ferric iron and sulphide ions, so-called iron–sulphur (Fe–S) clusters, are possibly nature’s most ancient prosthetic groups. One of the early actors in Fe–S cluster biosynthesis is a protein complex composed of a cysteine desulphurase, Nfs1, and its functional binding partner, Isd11. Although the essential function of Nfs1·Isd11 in the liberation of elemental sulphur from free cysteine is well established, little is known about its structure. Here, we provide evidence that shows Isd11 has a profound effect on the oligomeric state of Nfs1. |
| |
| Keywords: | Iron&ndash sulphur (Fe&ndash S) cluster assembly Mitochondria Saccharomyces cerevisiae Nfs1 Isd11 |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
