JACS 2016

A joint structural refinement against NMR data and X-ray diffraction patterns offers unique opportunities to detect differences in the conformation of biomolecules between the solution and the crystal states. Read More

ChemComm

An integrated approach which combines in-cell NMR spectroscopy with optical and X-ray fluorescence microscopy was developed to describe the intracellular maturation state of human Cu,Zn-SOD1.  Read More

NCB N terminal

Structural and biophysical evidences define the early steps of iron-sulfur protein maturation in the cytosol, demonstrating that  glutaredoxin-3 passes [2Fe-2S] clusters to anamorsin during a protein-protein interaction mediated by their N-terminal domains.  Read More 

nature chemistry

Dynamic nuclear polarization (DNP) in liquid solutions can enhance 13C NMR signals at magnetic fields of 3 T and room temperature up to three orders of magnitude. Read More  Highlighted in Angewandte Chemie

CERM research on covers

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High relaxivity Gd(III)-DNA gold nanostars: investigation of shape effects on proton relaxation, ACS nano, 9, 3385–3396, 2015 Exploring regions of conformational space occupied by two-domain proteins, J.Phys.Chem.B, 118, 10576-10587, 2014  

 

ChemComm

Combining in-cell NMR and X-ray fluorescence microscopy to reveal the intracellular maturation states of human superoxide dismutase 1

Luchinat E, Gianoncelli A, Mello T, Galli A, Banci L.

Chem Commun (Camb). 2015 Jan 11;51(3):584-7. doi: 10.1039/c4cc08129c. Epub 2014 Nov 21

Abstract

An integrated approach which combines in-cell NMR spectroscopy with optical and X-ray fluorescence microscopy was developed to describe the intracellular maturation state of human Cu,Zn-SOD1. Microscopy data show a correlation between the intracellular levels of SOD1 and the content of zinc, corresponding to zinc binding to SOD1 observed by in-cell NMR.

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NCB_full

Atomic-resolution monitoring of protein maturation in live human cells by NMR

Banci, L., Barbieri, L., Bertini, I., Luchinat, E., Secci, E., Zhao, Y., Aricescu, A.R.

Nat Chem Biol., 9, 297–299, 2013, . doi: 10.1038/nchembio.1202

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Abstract

We use NMR directly in live human cells to describe the complete post-translational maturation process of human superoxide dismutase 1 (SOD1). We follow, at atomic resolution, zinc binding, homodimer formation and copper uptake, and discover that copper chaperone for SOD1 oxidizes the SOD1 intrasubunit disulfide bond through both copper-dependent and copper-independent mechanisms. Our approach represents a new strategy for structural investigation of endogenously expressed proteins in a physiological (cellular) environment.

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The article has been evaluated on F1000 by:

Ad Bax on 9 Apr 2013

Joelle Pelletier on 3 Jul 2013

Michael Sattler and Lisa Warner on 13 Feb 2014.

 

 

PNAS

Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR

Banci, L., Bertini, I., Calderone, V., Cefaro, C., Ciofi-Baffoni, S., Gallo, A., Kallergi, E., Lionaki, E., Pozidis, C., Tokatlidis, K.

Proc Natl Acad Sci U S A. 2011 Mar 22;108(12):4811-6. doi:10.1073/pnas.1014542108.

Abstract

Oxidative protein folding in the mitochondrial intermembrane space requires the transfer of a disulfide bond from MIA40 to the substrate. During this process MIA40 is reduced and regenerated to a functional state through the interaction with the flavin-dependent sulfhydryl oxidase ALR. Here we present the mechanistic basis of ALR-MIA40 interaction at atomic resolution by biochemical and structural analyses of the mitochondrial ALR isoform and its covalent mixed disulfide intermediate with MIA40. This ALR isoform contains a folded FAD-binding domain at the C-terminus and an unstructured, flexible N-terminal domain, weakly and transiently interacting one with the other. A specific region of the N-terminal domain guides the interaction with the MIA40 substrate binding cleft (mimicking the interaction of the substrate itself), without being involved in the import of ALR. The hydrophobicity-driven binding of this region ensures precise protein-protein recognition needed for an efficient electron transfer process.

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