The anatomy of a bifunctional enzyme: structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1

Article Abstract:

The cytochrome cd1-nitrate reductase is a bifunctional enzyme which reduces oxygen to water and nitrite to NO. The cytochrome is a dimere and each subunit has a c and a d heme. The c heme is covalently bound and the electrons from the donors enter here. The d1 heme is noncovalently bound and the reduction of oxygen and nitrite takes place here. The movement of the two hemes, c and d1, that are situated in different domains play crucial roles in catalytic mechanism.

Cytochromes

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The 1.85 angstrom structure of vaccinia protein VP39: a bifunctional enzyme that participates in the modification of both mRNA ends

Article Abstract:

The 1.85 angstrom X-ray crystal structure of the AS11 mutant of VP39 bifunctional vaccinia virus protein complexed with its S-adenosylmethionine (AdoMet) cofactor is presented. VP39 acts as both an mRNA cap-specific RNA 2'-O-methyltransferase and a poly(A) polymerase processivity factor. Despite structural similarities to prokaryotic and eukaryotic methyltransferases, VP39 has a novel underlying architecture for an RNA-binding protein.

Chromosomal proteins, DNA viruses, Vaccinia

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Prolyl oligopeptidase: an unusual beta-propeller domain regulates proteolysis

Article Abstract:

A study was conducted to analyze prolyl oligopeptidase, a cytosolic enzyme belonging to a novel category of serine peptidases. The hanging-drop vapor diffusion method was carried out to determine prolyl oligopeptidase crystals. Results indicated that the enzyme supports a peptidase domain with an alpha/beta hydrolase fold. Findings also showed that its catalytic triad is covered by the central tunnel of a beta propeller.

Proteases, Oligopeptides

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