Protonation of the Binuclear Metal Center within the Active Site of Phosphotriesterase†

Biochemistry ◽  
2005 ◽  
Vol 44 (33) ◽  
pp. 11005-11013 ◽  
Author(s):  
Cynthia R. Samples ◽  
Timothy Howard ◽  
Frank M. Raushel ◽  
Victoria J. DeRose
Keyword(s):  
Active Site ◽  
Metal Center ◽  
Binuclear Metal

Evidence That Calcineurin Accommodates an Active Site Binuclear Metal Center

1995 ◽  
Vol 117 (40) ◽  
pp. 10147-10148 ◽  
Author(s):  
Lian Yu ◽  
Alice Haddy ◽  
Frank Rusnak
Keyword(s):  
Active Site ◽  
Metal Center ◽  
Binuclear Metal

scholarly journals Crystal structures of a ZIP zinc transporter reveal a binuclear metal center in the transport pathway

2017 ◽  
Vol 3 (8) ◽  
pp. e1700344 ◽  
Author(s):  
Tuo Zhang ◽  
Jian Liu ◽  
Matthias Fellner ◽  
Chi Zhang ◽  
Dexin Sui ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Zinc Transporter ◽  
Metal Center ◽  
Transport Pathway ◽  
Binuclear Metal

A combinatorial library for the binuclear metal center of bacterial phosphotriesterase

1997 ◽  
Vol 29 (4) ◽  
pp. 553-561 ◽  
Author(s):  
Linette M. Watkins ◽  
Jane M. Kuo ◽  
Misty Chen-Goodspeed ◽  
Frank M. Raushel
Keyword(s):  
Combinatorial Library ◽  
Metal Center ◽  
Binuclear Metal

Metallophosphoesterases: structural fidelity with functional promiscuity

2015 ◽  
Vol 467 (2) ◽  
pp. 201-216 ◽  
Author(s):  
Nishad Matange ◽  
Marjetka Podobnik ◽  
Sandhya S. Visweswariah
Keyword(s):  
Active Site ◽  
Metal Ion ◽  
Active Sites ◽  
Dependent Manner ◽  
The Core ◽  
Repair Enzymes ◽  
Phosphoprotein Phosphatases ◽  
Purple Acid Phosphatases ◽  
Binuclear Metal ◽  
Regulatory Effects

Calcineurin-like metallophosphoesterases (MPEs) form a large superfamily of binuclear metal-ion-centre-containing enzymes that hydrolyse phosphomono-, phosphodi- or phosphotri-esters in a metal-dependent manner. The MPE domain is found in Mre11/SbcD DNA-repair enzymes, mammalian phosphoprotein phosphatases, acid sphingomyelinases, purple acid phosphatases, nucleotidases and bacterial cyclic nucleotide phosphodiesterases. Despite this functional diversity, MPEs show a remarkably similar structural fold and active-site architecture. In the present review, we summarize the available structural, biochemical and functional information on these proteins. We also describe how diversification and specialization of the core MPE fold in various MPEs is achieved by amino acid substitution in their active sites, metal ions and regulatory effects of accessory domains. Finally, we discuss emerging roles of these proteins as non-catalytic protein-interaction scaffolds. Thus we view the MPE superfamily as a set of proteins with a highly conserved structural core that allows embellishment to result in dramatic and niche-specific diversification of function.

scholarly journals Structure of Diethyl Phosphate Bound to the Binuclear Metal Center of Phosphotriesterase†‡

Biochemistry ◽  
2008 ◽  
Vol 47 (36) ◽  
pp. 9497-9504 ◽  
Author(s):  
Jungwook Kim ◽  
Ping-Chuan Tsai ◽  
Shi-Lu Chen ◽  
Fahmi Himo ◽  
Steven C. Almo ◽  
...  
Keyword(s):  
Metal Center ◽  
Diethyl Phosphate ◽  
Binuclear Metal

Overexpression and Purification of Human Calcineurin α fromEscherichia coliand Assessment of Catalytic Functions of Residues Surrounding the Binuclear Metal Center†

Biochemistry ◽  
1997 ◽  
Vol 36 (16) ◽  
pp. 4934-4942 ◽  
Author(s):  
Angelo Mondragon ◽  
Eric C. Griffith ◽  
Luo Sun ◽  
Fei Xiong ◽  
Christopher Armstrong ◽  
...  
Keyword(s):  
Metal Center ◽  
Binuclear Metal ◽  
Catalytic Functions

scholarly journals Influence of the Greater Protein Environment on the Electrostatic Potential in Metalloenzyme Active Sites: the Case of Formate Dehydrogenase

2021 ◽  
Author(s):  
Azadeh Nazemi ◽  
Adam Steeves ◽  
Heather Kulik
Keyword(s):  
Electrostatic Potential ◽  
Active Site ◽  
Active Sites ◽  
Formate Dehydrogenase ◽  
Catalyst Design ◽  
Metal Center ◽  
Ambient Conditions ◽  
Shift Analysis ◽  
The Impact ◽  
Protein Environment

The Mo/W containing metalloenzyme formate dehydrogenase (FDH) is an efficient and selective natural catalyst which reversibly converts CO2 to formate under ambient conditions. A greater understanding of the role of the protein environment in determining the local properties of the FDH active site would enable rational bioinspired catalyst design. In this study, we investigate the impact of the greater protein environment on the electrostatic potential (ESP) of the active site. To model the enzyme environment, we used a combination of long-timescale classical molecular dynamics (MD) and multiscale quantum-mechanical/molecular-mechanical (QM/MM) simulations. We leverage the charge shift analysis method to systematically construct QM regions and analyze the electronic environment of the active site by evaluating the degree of charge transfer between the core active site and the protein environment. The contribution of the terminal chalcogen ligand to the ESP of the metal center is substantial and dependent on the chalcogen identity, with ESPs less negative and similar for Se and S terminal chalcogens than for O regardless of whether the Mo6+ or W6+ metal center is present. Our evaluation reveals that the orientation of the sidechains and ligand conformations will alter the relative trends in the ESP observed for a given metal center or terminal chalcogen, highlighting the importance of sampling dynamic fluctuations in the protein. Overall, our observations suggest that the terminal chalcogen ligand identity plays an important role in the enzymatic activity of FDH.

scholarly journals Asymmetric functions of a binuclear metal center within the transport pathway of a human zinc transporter ZIP4

2019 ◽  
Vol 34 (1) ◽  
pp. 237-247 ◽  
Author(s):  
Tuo Zhang ◽  
Dexin Sui ◽  
Chi Zhang ◽  
Logan Cole ◽  
Jian Hu
Keyword(s):  
Zinc Transporter ◽  
Metal Center ◽  
Transport Pathway ◽  
Binuclear Metal
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