An Extremely Stable Interprotein Tetrahedral Hg(Cys) Core Forms in the Zinc Hook Domain of Rad50 Protein at Physiological pH.

Invited for the cover of this issue is the group of Artur Krężel at the University of Wrocław in collaboration with Lars Hemmingsen at The University of Copenhagen and Eva Freisinger at the University of Zürich. The image depicts the outcomes of Hg interactions with Rad50 protein. Read the full text of the article at 10.

An Extremely Stable Interprotein Tetrahedral Hg(Cys) Core Forms in the Zinc Hook Domain of Rad50 Protein at Physiological pH.

In nature, thiolate-based systems are the primary targets of divalent mercury (Hg ) toxicity. The formation of Hg(Cys) cores in catalytic and structural protein centers mediates mercury's toxic effects and ultimately leads to cellular damage. Multiple studies have revealed distinct Hg -thiolate coordination preferences, among which linear Hg complexes are the most commonly observed in solution at physiological pH.

Conformational triggers associated with influenza matrix protein 1 polymerization.

A central role for the influenza matrix protein 1 (M1) is to form a polymeric coat on the inner leaflet of the host membrane that ultimately provides shape and stability to the virion. M1 polymerizes upon binding membranes, but triggers for conversion of M1 from a water-soluble component of the nucleus and cytosol into an oligomer at the membrane surface are unknown. While full-length M1 is required for virus viability, the N-terminal domain (M1NT) retains membrane binding and pH-dependent oligomerization.

Deciphering the Enigmatic Function of Metallothioneins.

Metallothioneins (MTs) are low molecular weight, Cys-rich proteins that sequester both essential and non-essential metal ions. Despite being highly conserved in the genus of Gram-negative bacteria, knowledge of their physiological function in this species is scarce. Using the strain Q2-87 as a model organism, we investigated the role of a conserved MT in zinc homeostasis, cadmium detoxification as well as its implications in stress response.

The Hepatitis B Virus Envelope Proteins: Molecular Gymnastics Throughout the Viral Life Cycle.

New hepatitis B virions released from infected hepatocytes are the result of an intricate maturation process that starts with the formation of the nucleocapsid providing a confined space where the viral DNA genome is synthesized via reverse transcription. Virion assembly is finalized by the enclosure of the icosahedral nucleocapsid within a heterogeneous envelope. The latter contains integral membrane proteins of three sizes, collectively known as hepatitis B surface antigen, and adopts multiple conformations in the course of the viral life cycle.

Impact of naturally occurring serine/cysteine variations on the structure and function of Pseudomonas metallothioneins.

Metallothioneins (MTs), small cysteine-rich metal-binding proteins, support the viability of organisms under normal physiological conditions and help them to respond to different environmental stressors. Upon metal coordination (e.g.

A histidine-rich Pseudomonas metallothionein with a disordered tail displays higher binding capacity for cadmium than zinc.

Metallothioneins (MTs) are crucial players in metal-related physiological processes. They are characterized by a high cysteine content and unique metal binding properties resulting in specific metal-thiolate clusters formation. Here we present the first NMR solution structure of a Pseudomonas MT, PflQ2 MT, using the strain P.

Effect of the Cation Distribution and Microstructure on the Magnetic Behavior of the CoMnO Oxide.

The sizes of CoMnO nanoparticles can easily be tuned, from 40 to 8 nm, depending on the temperature of decomposition of the single-source molecular precursor {[Co(bpy)][Mn(CO)]·HO}. The structural features of the CoMnO spinel are also affected by the heat treatment temperature, showing a pronounced expansion of unit cell parameters as a consequence of thermally induced cation redistribution between tetrahedral and octahedral sites. Moreover, the magnetic behavior of CoMnO was successfully tailored as well; depending on the heat treatment, it is possible to switch between the superparamagnetic and ferrimagnetic ordering and to tailor the magnetic transition temperatures, i.

A 3D oxalate-based network as a precursor for the CoMn₂O₄ spinel: synthesis and structural and magnetic studies.

A novel heterometallic oxalate-based compound of the formula {[Co(bpy)3][Mn2(C2O4)3]·H2O}n (1; bpy = 2,2'-bipyridine) was synthesized and characterized by elemental analysis, IR spectroscopy, single-crystal X-ray diffraction (XRD), and magnetization measurement. The molecular structure of 1 is made of a three-dimensional (3D) anionic network, [Mn2(C2O4)3]n(2n-), and tris-chelated cations [Co(bpy)3](2+) occupying the vacancies of the framework. Splitting between the zero-field-cooled (ZFC) and field-cooled (FC) branches of susceptibility below the small peak at 13 K indicates magnetic ordering.

Design of a peptidic turn with high affinity for Hg(II).

A four amino acid peptide containing the β-turn template dPro-Pro in the middle and two cysteines (Cys) in the terminal positions (CdPPC) has been synthesized and its mercury(II) coordination properties studied using different spectroscopic methods. The UV-vis, CD, (199m)Hg PAC, and Raman spectroscopic studies indicate the binding of Hg(II) to the two Cys, forming the dithiolatemercury(II) complex Hg(CdPPC). Electrospray ionization mass spectrometry corroborates the 1:1 complex formation.