TY - JOUR
T1 - Structure and Metal binding Characterization of the C-terminal Mellochaperone Domain of Membrane Fusion Protein SilB from Cupriavidus metallidurans CH34
AU - Bersch, Beate
AU - Derfoufi, Kheiro-mouna
AU - de Angelis, Fabien
AU - Auquier, Vanessa
AU - Ngonlong Ekende, Elisabeth
AU - Mergeay, Max
AU - Ruysschaert, Jean-Marie
AU - Vandenbussche, Guy
A2 - Monsieurs, Pieter
N1 - Score = 10
PY - 2011/2/7
Y1 - 2011/2/7
N2 - In Cupriavidus metallidurans CH34, a model organism for heavy metal resistance studies, the sil determinant is potentially involved in the efflux of of silver and copper ions. Proteins SilA, SilB, SilC form a resistance/nodulation/cell division (RND)-based transport system in which SilB is the periplasmic adaptor protein belonging to the membrane fusion protein family. In addition sto the four domains typical of known MFPs, SilB has a fifth additional C-terminal domain , SilB440-521. Structure and backbone of SilB440-521 have been investigated using NMR, and the residues of the metal site have been from 15N- and 13C-edited HSQC spectra.The solution structure and additional metal binding experiments that this C-terminal domain folds independantly of the rest of the protein and has a conformation and a Ag+ /Cu+ binding specificity similar to those determined for CusF from Escherichia coli. The samll protein CusF plays a role in metal trafficking in the periplasm. This suggests a potential metallochaperone role for SilB440-521 that is discussed in the context of simultaneous expression of different determinants involved in copper resistance in C.metallidurans CH34
AB - In Cupriavidus metallidurans CH34, a model organism for heavy metal resistance studies, the sil determinant is potentially involved in the efflux of of silver and copper ions. Proteins SilA, SilB, SilC form a resistance/nodulation/cell division (RND)-based transport system in which SilB is the periplasmic adaptor protein belonging to the membrane fusion protein family. In addition sto the four domains typical of known MFPs, SilB has a fifth additional C-terminal domain , SilB440-521. Structure and backbone of SilB440-521 have been investigated using NMR, and the residues of the metal site have been from 15N- and 13C-edited HSQC spectra.The solution structure and additional metal binding experiments that this C-terminal domain folds independantly of the rest of the protein and has a conformation and a Ag+ /Cu+ binding specificity similar to those determined for CusF from Escherichia coli. The samll protein CusF plays a role in metal trafficking in the periplasm. This suggests a potential metallochaperone role for SilB440-521 that is discussed in the context of simultaneous expression of different determinants involved in copper resistance in C.metallidurans CH34
KW - Cupriavidus metallidurans
KW - resistance to silver
KW - copper
KW - SilB Membrane Fusion protein
KW - efflux
KW - structure
KW - metallochaperone
KW - NMR
KW - HSQC spectra
UR - http://ecm.sckcen.be/OTCS/llisapi.dll/open/ezp_116208
UR - http://ecm.sckcen.be/OTCS/llisapi.dll/open/ezp_116208_2
UR - http://knowledgecentre.sckcen.be/so2/bibref/8381
U2 - 10.1021/bi200005k
DO - 10.1021/bi200005k
M3 - Article
SN - 0006-2960
VL - 50
SP - 2194
EP - 2204
JO - Biochemistry
JF - Biochemistry
IS - 12
ER -