2003
DOI: 10.1073/pnas.0932597100
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High-resolution structure of RNase P protein from Thermotoga maritima

Abstract: The structure of RNase P protein from the hyperthermophilic bacterium Thermotoga maritima was determined at 1.2-Å resolution by using x-ray crystallography. This protein structure is from an ancestral-type RNase P and bears remarkable similarity to the recently determined structures of RNase P proteins from bacteria that have the distinct, Bacillus type of RNase P. These two types of protein span the extent of bacterial RNase P diversity, so the results generalize the structure of the bacterial RNase P protein… Show more

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Cited by 86 publications
(68 citation statements)
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“…These structures reveal that bacterial RNase P proteins share a fold and structure similar to that of the prototypical B. subtilis protein, with an overall abbbaba topology and two RNA binding regions (central cleft and RNR motif) ( Fig. 1; Stams et al 1998;Spitzfaden et al 2000;Kazantsev et al 2003). The central cleft is formed by the central b-sheet and an a-helix (Stams et al 1998).…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation
“…These structures reveal that bacterial RNase P proteins share a fold and structure similar to that of the prototypical B. subtilis protein, with an overall abbbaba topology and two RNA binding regions (central cleft and RNR motif) ( Fig. 1; Stams et al 1998;Spitzfaden et al 2000;Kazantsev et al 2003). The central cleft is formed by the central b-sheet and an a-helix (Stams et al 1998).…”
Section: Introductionmentioning
confidence: 99%
“…The structures of several bacterial RNase P proteins have been solved by X-ray crystallography or NMR spectroscopy (Stams et al 1998;Spitzfaden et al 2000;Kazantsev et al 2003). These structures reveal that bacterial RNase P proteins share a fold and structure similar to that of the prototypical B. subtilis protein, with an overall abbbaba topology and two RNA binding regions (central cleft and RNR motif) ( Fig.…”
Section: Introductionmentioning
confidence: 99%
“…The structural organization of bacterial RNase P, which consists of a phylogenetically conserved catalytic RNA and a small protein has been established, and 1 several structures of the protein (Stams et al 1998;Spitzfaden et al 2000;Kazantsev et al 2003), RNA (Krasilnikov et al 2003(Krasilnikov et al , 2004Kazantsev et al 2005;Torres-Larios et al 2005), and holoenzymes (Reiter et al 2010;Kazantsev et al 2011) are available. At the same time, the structural organizations of the much more complex eukaryotic RNases MRP and P are not clear (Esakova and Krasilnikov 2010).…”
Section: Introductionmentioning
confidence: 99%
“…Crystal structures have been determined for independently folding ''catalytic'' (C-domain) and ''specificity'' (S-domain) structural domains of the A-and B-types of the bacterial ribozymes (Krasilnikov et al 2003(Krasilnikov et al , 2004Kazantsev et al 2009), for two full-size A-and B-type RNAs (Kazantsev et al 2005;Torres-Larios et al 2005) and, more recently, for the ternary complex between the A-type holoenzyme and the product tRNA (Reiter et al 2010). In addition, crystal structures of bacterial (Stams et al 1998;Spitzfaden et al 2000;Kazantsev et al 2003) and archaeal RNase P protein components (for review, see Evans et al 2006) have been solved, as well as a complex of two eucaryal proteins with a peripheral RNA fragment (Perederina et al 2010).…”
Section: Introductionmentioning
confidence: 99%