Proline Isomerization and Molten Globular Property of TgPDCD5 Secreted from Confers Its Regulation of Heparin Sulfate Binding.

Toxoplasmosis, caused by , poses risks to vulnerable populations. TgPDCD5, a secreted protein of , induces apoptosis through heparan sulfate-mediated endocytosis. The entry mechanism of TgPDCD5 has remained elusive.

Structural insight into the ZFAND1-p97 interaction involved in stress granule clearance.

Arsenite-induced stress granule (SG) formation can be cleared by the ubiquitin-proteasome system aided by the ATP-dependent unfoldase p97. ZFAND1 participates in this pathway by recruiting p97 to trigger SG clearance. ZFAND1 contains two An1-type zinc finger domains (ZF1 and ZF2), followed by a ubiquitin-like domain (UBL); but their structures are not experimentally determined.

NMR resonance assignments of the programmed cell death protein 5 (PDCD5) from Toxoplasma gondii.

Toxoplasmosis is a systematic protozoan disease caused by a tiny parasite Toxoplasma gondii. The infection can be dangerous for pregnant woman and people with weak immune systems. The secreted protein named TgPDCD5 (Programmed cell death protein 5 from Toxoplasma gondii) plays an important role in apoptosis-inducing effect on host cells.

High sensitivity high-resolution full range relaxometry using a fast mechanical sample shuttling device and a cryo-probe.

Field-dependent NMR studies of bio-molecular systems using a sample shuttling hardware operating on a high-field NMR apparatus have provided valuable structural and dynamic information. We have recently published a design of a compact sample transportation device, called "field-cycler", which was installed in a commercial spectrometer and which provided highly precise positioning and stability during high speed shuttling. In this communication, we demonstrate the first use of a sample shuttling device on a commercial high field standard bore NMR spectrometer, equipped with a commercial triple resonance cryogenically cooled NMR probe.

Structural dynamics of the two-component response regulator RstA in recognition of promoter DNA element.

The RstA/RstB system is a bacterial two-component regulatory system consisting of the membrane sensor, RstB and its cognate response regulator (RR) RstA. The RstA of Klebsiella pneumoniae (kpRstA) consists of an N-terminal receiver domain (RD, residues 1-119) and a C-terminal DNA-binding domain (DBD, residues 130-236). Phosphorylation of kpRstA induces dimerization, which allows two kpRstA DBDs to bind to a tandem repeat, called the RstA box, and regulate the expression of downstream genes.

(1)H, (13)C and (15)N resonance assignments of the C-terminal DNA-binding domain of RstA protein from Klebsiella pneumoniae.

Bacterial cells often use two-component signal transduction systems to regulate genes in response to environmental stimuli. The RstA/RstB system is a two-component regulatory system consisting of the membrane sensor, RstB, and its cognate response regulator RstA. The RstA of Klebsiella pneumoniae consists of a N-terminal receiver domain (NRD, residues 1-119) and a C-terminal DNA-binding domain (DBD, residues 130-236).

Disulfide pairings and secondary structure of porcine beta-microseminoprotein.

A sperm motility inhibitor isolated from porcine seminal plasma is identical to porcine beta-microseminoprotein (MSP). Circular dichroism (CD) and nuclear magnetic resonance (NMR) data showed that the native and recombinant porcine MSPs exhibit very similar structure. The five disulfide pairings on porcine MSP were unambiguously assigned based on NMR data and further confirmed using structural calculations.