2KI7

The solution structure of RPP29-RPP21 complex from Pyrococcus furiosus

Summary for 2KI7

• Entry DOI: 10.2210/pdb2ki7/pdb
• Descriptor: Ribonuclease P protein component 1, Ribonuclease P protein component 4, ZINC ION (3 entities in total)
• Functional Keywords: rnase p, hydrolase, trna processing
• Biological source: Pyrococcus furiosus DSM 3638; More
• Total number of polymer chains: 2
• Total formula weight: 29969.96

Authors

Xu, Y.,Foster, M.P. (deposition date: 2009-04-28, release date: 2009-09-15, Last modification date: 2024-05-22)

Primary citation

Xu, Y.,Amero, C.D.,Pulukkunat, D.K.,Gopalan, V.,Foster, M.P.
Solution structure of an archaeal RNase P binary protein complex: formation of the 30-kDa complex between Pyrococcus furiosus RPP21 and RPP29 is accompanied by coupled protein folding and highlights critical features for protein-protein and protein-RNA interactions.
J.Mol.Biol., 393:1043-1055, 2009

PubMed Abstract: Ribonuclease P (RNase P) is a ribonucleoprotein (RNP) enzyme that catalyzes the Mg(2+)-dependent 5' maturation of precursor tRNAs. In all domains of life, it is a ribozyme: the RNase P RNA (RPR) component has been demonstrated to be responsible for catalysis. However, the number of RNase P protein subunits (RPPs) varies from 1 in bacteria to 9 or 10 in eukarya. The archaeal RPR is associated with at least 4 RPPs, which function in pairs (RPP21-RPP29 and RPP30-POP5). We used solution NMR spectroscopy to determine the three-dimensional structure of the protein-protein complex comprising Pyrococcus furiosus RPP21 and RPP29. We found that the protein-protein interaction is characterized by coupled folding of secondary structural elements that participate in interface formation. In addition to detailing the intermolecular contacts that stabilize this 30-kDa binary complex, the structure identifies surfaces rich in conserved basic residues likely vital for recognition of the RPR and/or precursor tRNA. Furthermore, enzymatic footprinting experiments allowed us to localize the RPP21-RPP29 complex to the specificity domain of the RPR. These findings provide valuable new insights into mechanisms of RNP assembly and serve as important steps towards a three-dimensional model of this ancient RNP enzyme.

PubMed: 19733182
DOI: 10.1016/j.jmb.2009.08.068

Experimental method

SOLUTION NMR