Longitudinal study of SARS-CoV-2 infections in different employee groups of long distance train services from June 2020 until February 2021 in Germany.

This prospective longitudinal epidemiological study was aimed at investigating the occupational SARS-CoV-2 infection risk of long distance train services in Germany. Three different employee groups (train attendants, train drivers and maintenance workers) within the workforce of the German railway carrier Deutsche Bahn Fernverkehr AG were studied based on their contact frequency with passengers and colleagues. Approximately 1100 employees were tested by PCR for acute infections and by antibody detection for past infections in June 2020, October 2020 and February 2021.

Crystal structures of human saposins C andD: implications for lipid recognition and membrane interactions.

Human saposins are essential proteins required for degradation of sphingolipids and lipid antigen presentation. Despite the conserved structural organization of saposins, their distinct modes of interaction with biological membranes are not fully understood. We describe two crystal structures of human saposin C in an "open" configuration with unusual domain swapped homodimers.

Crystallization and preliminary characterization of three different crystal forms of human saposin C heterologously expressed in Pichia pastoris.

The amphiphilic saposin proteins (A, B, C and D) act at the lipid-water interface in lysosomes, mediating the hydrolysis of membrane building blocks by water-soluble exohydrolases. Human saposin C activates glucocerebrosidase and beta-galactosylceramidase. The protein has been expressed in Pichia pastoris, purified and crystallized in three different crystal forms, diffracting to a maximum resolution of 2.

Conjugated bile acid hydrolase is a tetrameric N-terminal thiol hydrolase with specific recognition of its cholyl but not of its tauryl product.

Bacterial bile salt hydrolases catalyze the degradation of conjugated bile acids in the mammalian gut. The crystal structures of conjugated bile acid hydrolase (CBAH) from Clostridium perfringens as apoenzyme and in complex with taurodeoxycholate that was hydrolyzed to the reaction products taurine and deoxycholate are described here at 2.1 and 1.

A large hinge bending domain rotation is necessary for the catalytic function of Escherichia coli 5'-nucleotidase.

Two variants of Escherichia coli 5'-nucleotidase with disulfide bridges that were engineered to link the two domains of the protein were used to demonstrate that a large domain rotation is required for the catalytic mechanism of the enzyme. Kinetic analysis demonstrates that the variant trapped in the open form is almost inactive but can be activated up to 250-fold by reduction of the disulfide bridge. The second variant can adopt a closed but also a half-open conformation despite the presence of the cystine linkage.

Trapping a 96 degrees domain rotation in two distinct conformations by engineered disulfide bridges.

Engineering disulfide bridges is a common technique to lock a protein movement in a defined conformational state. We have designed two double mutants of Escherichia coli 5'-nucleotidase to trap the enzyme in both an open (S228C, P513C) and a closed (P90C, L424C) conformation by the formation of disulfide bridges. The mutant proteins have been expressed, purified, and crystallized, to structurally characterize the designed variants.