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By Alton Meister

Chemical and Genetic Probes of the lively website of D-Ribulose-1,5-Bifphosphate Carboxylase/Oxygenase: A Retrospective according to the 3-dimensional constitution (F. Hartman & M. Harpel).

Phenylalanine Hydroxylating approach (S. Kaufman).

Post-Translational amendment of Proteins (R. Krishna & F. Wold).

The position of steel Clusters and MgATP in Nitrogenase Catalysis (L. Mortenson, et al.).

Myristoyl CoA: Protein N-Myristoyl-Transferase (D. Rudnick, et al.).

improvement of Enzyme-Based equipment for DNA series research and Their functions within the Genome tasks (R. Wu).

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At first glance, the crystal structure of the activated form of the R. rubrum enzymeaRuBP complex would appear ideal for visualizing the active- 52 FRED C. HARTMAN AND MARK R. HARPEL site side chains as positioned at commencement of the catalytic cycle (84). In actuality, the situation is less straightforward because the “activated” enzymewbstrate complex is inactive. In one of the two subunits in the dimeric molecule, loop 6 is locked in the open conformation by intermolecular electrostatic interactions, which could explain the catalytic incompetence of that subunit.

HARTMAN AND MARK R. HARPEL site side chains as positioned at commencement of the catalytic cycle (84). In actuality, the situation is less straightforward because the “activated” enzymewbstrate complex is inactive. In one of the two subunits in the dimeric molecule, loop 6 is locked in the open conformation by intermolecular electrostatic interactions, which could explain the catalytic incompetence of that subunit. However, loop 6 is not observed in the electron density map of the second subunit, indicative of the mobility necessary for catalysis.

The R. rubrum enzyme was first cloned as a fusion protein that contained a 25-residue N-terminal appendage (120). As the fusion protein appeared catalytically identical to wild-type, all of the crystallographic analyses of the L2 Rubisco discussed in a preceding section were carried out with this material. The appendage, not seen in the electron density map, must be unstructured and irrelevant to proper folding. However, much of the mutagenesis has relied on a reconstruction of the original clone that encodes authentic, wild-type enzyme (121).

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