2AQA: NMR structural analysis of Nop10p from Saccharomyces cerevisiae

Box H/ACA ribonucleoprotein particles (RNPs) catalyze RNA pseudouridylation and direct processing of ribosomal RNA, and are essential architectural components of vertebrate telomerases. H/ACA RNPs comprise four proteins and a multihelical RNA. Two proteins, Cbf5 and Nop10, suffice for basal enzymatic activity in an archaeal in vitro system. We now report their cocrystal structure at 1.95-A resolution. We find that archaeal Cbf5 can assemble with yeast Nop10 and with human telomerase RNA, consistent with the high sequence identity of the RNP components between archaea and eukarya. Thus, the Cbf5-Nop10 architecture is phylogenetically conserved. The structure shows how Nop10 buttresses the active site of Cbf5, and it reveals two basic troughs that bidirectionally extend the active site cleft. Mutagenesis results implicate an adjacent basic patch in RNA binding. This tripartite RNA-binding surface may function as a molecular bracket that organizes the multihelical H/ACA and telomerase RNAs.
PDB ID: 2AQADownload
MMDB ID: 36101
PDB Deposition Date: 2005/8/17
Updated in MMDB: 2005/12
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Molecular Components in 2AQA
Label Count Molecule
Protein (1 molecule)
H/aca Ribonucleoprotein Complex Subunit 3(Gene symbol: NOP10)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB