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metallochaperone complex

Known as: metallochaperone complex location 
A protein complex which is capable of metallochaperone activity. [GO_REF:0000088, GOC:bhm, GOC:TermGenie, PMID:10426947]
National Institutes of Health

Papers overview

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2019
2019
A solvent-exposed cysteine forms a peculiar Ni(II)-binding site in the metallochaperone CooT from Rhodospirillum rubrum.
In Rhodospirillum rubrum, the maturation of carbon monoxide dehydrogenase (CODH) requires three nickel chaperones, namely RrCooC… 
2019
2019
Metallochaperones Are Needed for Mycobacterium tuberculosis and Escherichia coli Nicotinamidase-Pyrazinamidase Activity
Tuberculosis is an infectious disease caused by the bacterium Mycobacterium tuberculosis and remains one of the major causes of… 
2018
2018
The Role of the Metallochaperone HypA in the Acid Survival and Activities of Nickel Enzymes in Helicobacter pylori
.................................................................................................................................... v LIST OF TABLES .......................................................................................................................... xi LIST OF FIGURES ....................................................................................................................... xii CHAPTER 
2013
2013
In vivo study of the interaction of bismuth-based drugs with metallochaperone HspA in Helicobacter pylori
2012
2012
Zinc Homeostasis in E. coli
ZINC HOMEOSTASIS IN E.COLI by M. Patrick Hensley The homeostasis of transition metal ions is critical to the survival of all… 
2011
2011
NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: insights on the role of methionine.
The first NMR structure of a Cu(I)-bound metallochaperone model with the conserved sequence MT/HCXXC revealed that at pH ∼3.0 and… 
Highly Cited
2009
Highly Cited
2009
Structure of a nickel chaperone, HypA, from Helicobacter pylori reveals two distinct metal binding sites.
Metallochaperones bind metals and ensure the safe delivery of metals to the targets. They are required for the activation and… 
2009
2009
NMR structural analysis of the soluble domain of ZiaA-ATPase and the basis of selective interactions with copper metallochaperone Atx1
A Cu(I) metallochaperone, Atx1, interacts with the amino-terminal domain of a Cu(I)-transporting ATPase, PacSN, but not with a… 
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