Open Access. Powered by Scholars. Published by Universities.®
Articles 1 - 3 of 3
Full-Text Articles in Life Sciences
Conformations Of The Apo-, Substrate-Bound And Phosphate-Bound Atp-Binding Domain Of The Cu(Ii) Atpase Copb Illustrate Coupling Of Domain Movement To The Catalytic Cycle, José Argüello, Samuel Jayakanthan, Sue Roberts, Andrzej Weichsel, Megan Mcevoy
Conformations Of The Apo-, Substrate-Bound And Phosphate-Bound Atp-Binding Domain Of The Cu(Ii) Atpase Copb Illustrate Coupling Of Domain Movement To The Catalytic Cycle, José Argüello, Samuel Jayakanthan, Sue Roberts, Andrzej Weichsel, Megan Mcevoy
José M. Argüello
Heavy metal P1B-type ATPases play a critical role in cell survival by maintaining appropriate intracellular metal concentrations. Archaeoglobus fulgidus CopB is a member of this family that transports Cu(II) from the cytoplasm to the exterior of the cell using ATP as energy source. CopB has a 264 amino acid ATPBD (ATP-binding domain) that is essential for ATP binding and hydrolysis as well as ultimately transducing the energy to the transmembrane metal-binding site for metal occlusion and export. The relevant conformations of this domain during the different steps of the catalytic cycle are still under discussion. Through crystal structures of the …
Identifying Metalloproteins Through X-Ray Fluorescence Mapping And Mass Spectrometry., José Argüello, Daniel Raimunda, Tripti Khare, Carol Giometti, Stefan Vogt, Lydia Finney
Identifying Metalloproteins Through X-Ray Fluorescence Mapping And Mass Spectrometry., José Argüello, Daniel Raimunda, Tripti Khare, Carol Giometti, Stefan Vogt, Lydia Finney
José M. Argüello
Metals are critical and dynamic components of biochemistry. To understand their roles, we greatly need tools to identify the ligands that bind them within the complexity of natural systems. This work describes the development of methods that not only detect and distinguish metals, but also characterize the proteins that bind them. We describe an approach to expose, identify and quantify metalloproteins in complex mixtures by sequential non-denaturing 2D-gel electrophoresis (2D GE)/X-ray Fluorescence (XRF) and tandem mass spectrometry (MS/MS) in the same spot of a sample. We first apply the development of 2D GE/XRF to Shewanella oneidensis MR-1, a well-studied system, …
Evolution And Diversity Of Periplasmic Proteins Involved In Copper Homeostasis In Gamma Proteobacteria., José Argüello, Georgina Hernandez-Montes, Brenda Valderrama
Evolution And Diversity Of Periplasmic Proteins Involved In Copper Homeostasis In Gamma Proteobacteria., José Argüello, Georgina Hernandez-Montes, Brenda Valderrama
José M. Argüello
Background: Different systems contributing to copper homeostasis in bacteria have been described in recent years involving periplasmic and transport proteins that provide resistance via metal efflux to the extracellular media (CopA/Cue, Cus, Cut, and Pco). The participation of these proteins in the assembly of membrane, periplasmic and secreted cuproproteins has also been postulated. The integration and interrelation of these systems and their apparent redundancies are less clear since they have been studied in alternative systems. Based on the idea that cellular copper is not free but rather it is transferred via protein-protein interactions, we hypothesized that systems would coevolve and …