3pla

Crystal structure of a catalytically active substrate-bound box C/D RNP from Sulfolobus solfataricus

spinqualitylabelsall models 3pla, resolution 3.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pla is a 15 chain structure with sequence from Saccharolobus solfataricus, Saccharolobus solfataricus 98/2 and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.15Å Ligands: SAH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D0KRE2_SACS9 Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, the RNA component of RNase P, box H/ACA, box C/D and box C'/D' sRNAs.[HAMAP-Rule:MF_00326] Publication Abstract from PubMed Box C/D RNA protein complexes (RNPs) direct site-specific 2'-O-methylation of RNA and ribosome assembly. The guide RNA in C/D RNP forms base pairs with complementary substrates and selects the modification site using a molecular ruler. Despite many studies of C/D RNP structure, the fundamental questions of how C/D RNAs assemble into RNPs and how they guide modification remain unresolved. Here we report the crystal structure of an entire catalytically active archaeal C/D RNP consisting of a bipartite C/D RNA associated with two substrates and two copies each of Nop5, L7Ae and fibrillarin at 3.15-A resolution. The substrate pairs with the second through the eleventh nucleotide of the 12-nucleotide guide, and the resultant duplex is bracketed in a channel with flexible ends. The methyltransferase fibrillarin binds to an undistorted A-form structure of the guide-substrate duplex and specifically loads the target ribose into the active site. Because interaction with the RNA duplex alone does not determine the site specificity, fibrillarin is further positioned by non-specific and specific protein interactions. Compared with the structure of the inactive C/D RNP, extensive domain movements are induced by substrate loading. Our results reveal the organization of a monomeric C/D RNP and the mechanism underlying its site-specific methylation activity. Structural basis for site-specific ribose methylation by box C/D RNA protein complexes.,Lin J, Lai S, Jia R, Xu A, Zhang L, Lu J, Ye K Nature. 2011 Jan 27;469(7331):559-563. PMID:21270896 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Kink-turn motif Ribosomal protein L7/L12 User:Wayne Decatur/kink-turn motif

Proteopedia Page Contributors and Editors (what is this?)

OCA