Staying on track: common features of DNA helicases and microtubule motors

Article Abstract:

A review was done to compare the mechanistic features of Escherichia coli Rep helicase and kinesin, which both function as homodimeric enzymes. Although these enzymes have different structures and operate on different polymers, they use mechanisms wherein one of the subunits of the dimer is bound tightly to the lattice while the second subunit moves forward to the next binding site. Subsequently, the two subunits exchange positions as the process is repeated for several times.

Escherichia coli, Kinesin

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The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site

Article Abstract:

The NS3 proteinase of the hepatitis C virus (HCV) exhibits a three-dimensional structure with folded beta barrels that are composed of six strands. The beta strands are connected by short loops composed of 140 amino acid residues and an alpha helix located in the 171-174 amino acid sequence. The HCV proteinase also exhibits an oxyanion-stabilizing loop with three catalytic residues that are arranged in spatial positions similar to other trypsin-like proteinases.

Hepatitis C virus

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Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments

Article Abstract:

A plausible model of the structure of the alpha-actinin rod is presented. The model was derived after the determination of the crystal structure of the two central repeats in the alpha-actinin rod at a resolution of 2.5 Angstroms. This molecular architecture, which places the actin-binding sides at both ends of the rod in an antiparallel fashion, is indicative of a protein that is capable of forming cross-links between actin filaments.

Actin, Protein research

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