Benoit Masquida and Eric Westhof
RNA 7, 1615-1618 (2011)
Masquida and Westhof who are both at Strasbourg, France, review the X-ray structure obtained with a resolution of 4.2 Angstroms of RNase P, a ribozyme like the ribosome which has the ability to work as a "multiple turnover" enzyme. The structure of RNase P has PDB_ID's: 3Q1Q and 3Q1R, the difference is that the second one contains the 5'-leader whereas the first comes without, and at 3.8 Angstrom resolution.
The structure was determined by a group of researchers at Northwestern University and the University of Chicago and the main author is Nicolas Reiter who is a post-doctoral researcher at Alfonso Mondragon's Lab at Northwestern. The reason for the review is mainly that Tsai, Masquida, Westhof and others proposed a structure for RNase P in 2003 from secondary structure maps enriched with hydroxyl-radical footprinting data and it's quite close to the final crystal structure. A pymol generated figure showing the full holoenzyme is drawn below:
Notice the 5'-leader is rendered as spheres with carbons in grey color and just in top of the protein part (drawn in black) of the holoenzyme (holoenzyme=enzyme+cofactors). The surface in blue is just given the name P-RNA, and the part rendered as sticks is pre-tRNAphe. The whole structure has a total of 423 bases coming from the P-RNA and the pre-tRNAphe.
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