6cwx | pdb_00006cwx

Crystal structure of human ribonuclease P/MRP proteins Rpp20/Rpp25

spinqualitylabelsall models 6cwx, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6cwx is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FMT, SO4 NonStd Res: CME Gene: POP7, RPP20 (HUMAN), RPP25 (HUMAN) Activity: Ribonuclease P, with EC number 3.1.26.5 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [POP7_HUMAN] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP complex, which cleaves pre-rRNA sequences. [RPP25_HUMAN] Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP. This subunit binds to RNA. Publication Abstract from PubMed RNase P catalyzes the removal of 5' leaders of tRNA precursors and its central catalytic RNA subunit is highly conserved across all domains of life. In eukaryotes, RNase P and RNase MRP, a closely related ribonucleoprotein enzyme, share several of the same protein subunits, contain a similar catalytic RNA core, and exhibit structural features that do not exist in their bacterial or archaeal counterparts. A unique feature of eukaryotic RNase P/MRP is the presence of two relatively long and unpaired internal loops within the P3 region of their RNA subunit bound by a heterodimeric protein complex, Rpp20/Rpp25. Here we present a crystal structure of the human Rpp20/Rpp25 heterodimer and we propose, using comparative structural analyses, that the evolutionary divergence of the single-stranded and helical nucleic acid binding specificities of eukaryotic Rpp20/Rpp25 and their related archaeal Alba chromatin protein dimers, respectively, originate primarily from quaternary level differences observed in their heterodimerization interface. Our work provides structural insights into how the archaeal Alba protein scaffold was adapted evolutionarily for incorporation into several functionally-independent eukaryotic ribonucleoprotein complexes. Crystal structure of human Rpp20/Rpp25 reveals quaternary level adaptation of the Alba scaffold as structural basis for single-stranded RNA binding.,Chan CW, Kiesel BR, Mondragon A J Mol Biol. 2018 Apr 3. pii: S0022-2836(18)30180-3. doi:, 10.1016/j.jmb.2018.03.029. PMID:29625199 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribonuclease 3D structures

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