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Nuclear magnetic resonance signal chemical shifts and molecular simulations: a multidisciplinary approach to modeling copper protein structures.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Sgrignani, Jacopo Pierattelli, Roberta
Description	Country affiliation: Italy Author Affiliation: Sgrignani J ( Magnetic Resonance Center (CERM) and Department of Chemistry Ugo Schiff, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy.)
Abstract	Nuclear magnetic resonance (NMR) chemical shifts are experimental observables that are available during the first stage of the protein structure determination process. Recently, some methodologies for building structural models of proteins using only these experimental data have been implemented. To assess the potential of these methods for modeling metalloproteins (generally considered a challenging benchmark), we determined the structures of the yeast copper chaperone Atx1 and the CuA domain of Thermus thermophilus cytochrome c oxidase starting from the available chemical shift data. The metal centers were modeled using molecular dynamics simulations with molecular mechanics potentials. The results obtained are evaluated and discussed.
File Format	HTM / HTML
ISSN	09498257
Issue Number	1
Volume Number	17
e-ISSN	14321327
Journal	JBIC Journal of Biological Inorganic Chemistry
Language	English
Publisher	Springer
Publisher Date	2012-01-01
Publisher Place	Germany
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biochemistry Carrier Proteins Chemistry Copper Cytochrome c Group Magnetic Resonance Spectroscopy Molecular Dynamics Simulation Saccharomyces Cerevisiae Proteins Metabolism Crystallography, X-ray Models, Molecular Protein Structure, Tertiary Saccharomyces Cerevisiae Enzymology Thermus Thermophilus Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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Crystal structure of Saccharomyces cerevisiae Aro8, a putative -aminoadipate aminotransferase.

Crystal structure of inorganic pyrophosphatase from Thermus thermophilus.

Structure and Mechanism of the Bifunctional CinA Enzyme from Thermus thermophilus $^{*}$

Structures of the autoproteolytic domain from the Saccharomyces cerevisiae nuclear pore complex component, Nup145.

Crystal structure of N-acylamino acid racemase from Thermus thermophilus HB8.

Structures of hypoxanthine-guanine phosphoribosyltransferase (TTHA0220) from Thermus thermophilus HB8

Crystal structure of the proline iminopeptidase-related protein TTHA1809 from Thermus thermophilus HB8.

Crystal structure of a predicted phosphoribosyltransferase (TT1426) from Thermus thermophilus HB8 at 2.01 Å resolution

Crystal and NMR structures give insights into the role and dynamics of subunit F of the eukaryotic V-ATPase from Saccharomyces cerevisiae.

Nuclear magnetic resonance signal chemical shifts and molecular simulations: a multidisciplinary approach to modeling copper protein structures.

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Crystal structure of Saccharomyces cerevisiae Aro8, a putative -aminoadipate aminotransferase.

Crystal structure of inorganic pyrophosphatase from Thermus thermophilus.

Structure and Mechanism of the Bifunctional CinA Enzyme from Thermus thermophilus $^{*}$

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Nuclear magnetic resonance signal chemical shifts and molecular simulations: a multidisciplinary approach to modeling copper protein structures.