INVESTIGADORES
VILA Alejandro Jose
artículos
Título:
A dimerization interface mediated by functionally critical residues creates interfacial disulfide bonds and copper sites in CueP
Autor/es:
ABRIATA LA; PONTEL L.B.; A. J. VILA; DAL PERARO, M; SONCINI, F
Revista:
JOURNAL OF INORGANIC BIOCHEMISTRY
Editorial:
ELSEVIER SCIENCE INC
Referencias:
Lugar: Amsterdam; Año: 2014
ISSN:
0162-0134
Resumen:
CueP confers bacterial copper resistance in the periplasm, particularly
under anaerobic conditions, through an unknown mechanism. The only
available structure and limited solution data suggest that CueP forms
noncovalent dimers in solution, whereas sequence conservation suggests
important roles for three cysteines and two histidines as copper
ligands. Here we report evidence of a dimerization equilibrium mediated
by a newly identified interface of functional relevance, which occludes
internal copper sites and disulfide bonds but allows for intra- and
interchain disulfide bonding, an extensive disulfide relay, and
interfacial copper sites. Our results suggest a role for CueP linking
redox-state sensing and copper detoxification.