The proteasome: paradigm of a self-compartmentalizing protease

Article Abstract:

The structure of self-compartmentalizing proteases are characterized by mechanisms of action and protein degradations. The core structure is characterized by subunits arranged into four seven-membered rings and noncatalytic alpha and catalytic beta-type subunits having the same fold. Moreover, the assembly of the 20S proteasome is directly associated with the processing of the beta-type subunits. The alpha rings function as a template wherein the beta subunits assemble after the formation of a ring containing all of the seven alpha-type subunits.

Proteins, Protein structure

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Crystal and solution structures of an HslUV protease-chaperone complex

Article Abstract:

Research describes the crystal and solution structure of an heat shock locus gene products U and V complex of influenza virus. Data reveal that HsIU ATPase and HsIV protease of the complex bear 80% amino acid sequence homology to the Escherichia coli counterparts.

Heat shock proteins, Adenosine triphosphatase, Influenza viruses

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Cocrystal structure of a tRNA Psi55 pseudouridine synthase: nucleotide flipping by an RNA-modifying enzyme

Article Abstract:

The crystal structure of Psi synthase TruB bound to RNA shows that the enzyme recognizes T loop through shape complementarity. The enzyme accesses the uridyl substrate by flipping out the nucleotides, which disrupts the tRNA tertiary structure.

Enzymes, RNA, Isomerization, Enzyme structure-activity relationships

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