5MTZ

Crystal structure of a long form RNase Z from yeast

Summary for 5MTZ

• Entry DOI: 10.2210/pdb5mtz/pdb
• Descriptor: Ribonuclease Z, ZINC ION, PHOSPHATE ION (3 entities in total)
• Functional Keywords: zinc-dependent metal hydrolase, hydrolase, ribonuclease z
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Cytoplasm : P36159
• Total number of polymer chains: 2
• Total formula weight: 204484.23

Authors

Li de la Sierra-Gallay, I.,Miao, M.,van Tilbeurgh, H. (deposition date: 2017-01-11, release date: 2017-06-21, Last modification date: 2024-11-06)

Primary citation

Ma, M.,Li de la Sierra-Gallay, I.,Lazar, N.,Pellegrini, O.,Durand, D.,Marchfelder, A.,Condon, C.,van Tilbeurgh, H.
The crystal structure of Trz1, the long form RNase Z from yeast.
Nucleic Acids Res., 45:6209-6216, 2017

PubMed Abstract: tRNAs are synthesized as precursor RNAs that have to undergo processing steps to become functional. Yeast Trz1 is a key endoribonuclease involved in the 3΄ maturation of tRNAs in all domains of life. It is a member of the β-lactamase family of RNases, characterized by an HxHxDH sequence motif involved in coordination of catalytic Zn-ions. The RNase Z family consists of two subfamilies: the short (250-400 residues) and the long forms (about double in size). Short form RNase Z enzymes act as homodimers: one subunit embraces tRNA with a protruding arm, while the other provides the catalytic site. The long form is thought to contain two fused β-lactamase domains within a single polypeptide. Only structures of short form RNase Z enzymes are known. Here we present the 3.1 Å crystal structure of the long-form Trz1 from Saccharomyces cerevisiae. Trz1 is organized into two β-lactamase domains connected by a long linker. The N-terminal domain has lost its catalytic residues, but retains the long flexible arm that is important for tRNA binding, while it is the other way around in the C-terminal domain. Trz1 likely evolved from a duplication and fusion of the gene encoding the monomeric short form RNase Z.

PubMed: 28379452
DOI: 10.1093/nar/gkx216

Experimental method

X-RAY DIFFRACTION (2.99 Å)