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Your search keyword '"Bertini, Ivano"' showing total 23 results
Start Over Author "Bertini, Ivano" Journal journal of biological chemistry
23 results on '"Bertini, Ivano"'

19. Backbone Dynamics of Plastocyanin in Both Oxidation States

Author

Bertini, Ivano, primary, Bryant, Donald A., additional, Ciurli, Stefano, additional, Dikiy, Alexander, additional, Fernández, Claudio O., additional, Luchinat, Claudio, additional, Safarov, Niyaz, additional, Vila, Alejandro J., additional, and Zhao, Jindong, additional

Published
2001
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22. An NMR Study of the Interaction of the N-terminal Cytoplasmic Tail of the Wilson Disease Protein with Copper(l)-HAH1.

Author

Lucia Banci, Bertini, Ivano, Cantini, Francesca, Massagni, Chiara, Migliardi, Manuele, and Rosato, Antonio

Subjects
*NUCLEAR magnetic resonance spectroscopy, *HEPATOLENTICULAR degeneration, *ADENOSINE triphosphate, *BACTERIAL genetics, *ESCHERICHIA coli, *MOLECULAR chaperones, *CYTOPLASM, *HOMEOSTASIS, *GENETICS
Abstract

ATP7B is a human P15-type ATPase that has a crucial role in maintaining copper(I) homeostasis. Mutations in the corresponding gene are the cause of Wilson disease. Among its various distinguishing features is a long (∼630 amino acids) N-terminal cytosolic tail containing six domains that are individually folded and capable of binding one copper(I) ion each, We expressed the entire tail as a single construct in Escherichia coli and investigated its interaction with its copper chaperone (i.e. HAH1) by solution NMR spectroscopy. We observed that all six of the metal-binding domains were metallated by Cu(I)-HAH1, with the first, the second, and the fourth domains forming an adduct with it, This behavior is different from that of the highly similar human ATPase ATP7A, in which only two domains form such an adduct. The distinct behaviors of the different domains were analyzed in terms of the energetics of Cu(I) transfer, hinting at a specific role of the interaction with copper(I)-HAH1 in the overall functional process. [ABSTRACT FROM AUTHOR]

Published
2009
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23. Solution Structure of Cox11, a Novel type of β-Immunoglobulin-like Fold Involved in CuB Site Formation of Cytochrome c Oxidase.

Author

Banci, Lucia, Bertini, Ivano, Cantini, Francesca, Ciofi-Baffoni, Simone, Gonnelli, Leonardo, and Mangani, Stefano

Subjects
*CYTOCHROME c, *OXIDASES, *PROTEINS, *GENOMES, *AMINO acids, *BIOLOGICAL membranes
Abstract

Cytochrome c oxidase assembly process involves many accessory proteins including Cox11, which is a copper-binding protein required for Cu incorporation into the CuB site of cytochrome c oxidase. In a genome wide search, a number of Cox11 homologs are found in all of the eukaryotes with complete genomes and in several Gram-negative bacteria. All of them possess a highly homologous soluble domain and contain an N-terminal fragment that anchors the protein to the membrane. An anchor-free construct of 164 amino acids was obtained from Sinorhizobium meliloti, and the first structure of this class of proteins is reported here. The apoform has an immunoglobulin-like fold with a novel type of β-strand organization. The copper binding motif composed of two highly conserved cysteines is located on one side of the β-barrel structure. The apoprotein is monomeric in the presence of dithiothreitol, whereas it dimerizes in the absence of the reductant. When copper(I) binds, NMR and extended x-ray absorption fine structure (EXAFS) data indicate a dimeric protein state with two thiolates bridging two copper(I) ions. The present results advance the knowledge on the poorly understood molecular aspects of cytochrome c oxidase assembly. [ABSTRACT FROM AUTHOR]

Published
2004
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