3LWQ

Structure of H/ACA RNP bound to a substrate RNA containing 3MU

Summary for 3LWQ

• Entry DOI: 10.2210/pdb3lwq/pdb
• Related: 3LWO 3LWP 3LWR 3LWV
• Descriptor: Probable tRNA pseudouridine synthase B, Ribosome biogenesis protein Nop10, Large ribosomal subunit protein eL8, ... (6 entities in total)
• Functional Keywords: h/aca pseudouridine synthase, isomerase, trna processing, ribonucleoprotein, ribosome biogenesis, rrna processing, ribosomal protein, rna-binding, isomerase-rna binding protein-rna complex, isomerase/rna binding protein/rna
• Biological source: Pyrococcus furiosus; More
• Total number of polymer chains: 5
• Total formula weight: 82239.45

Authors

Zhou, J.,Liang, B.,Lv, C.,Yang, W.,Li, H. (deposition date: 2010-02-24, release date: 2010-07-14, Last modification date: 2024-11-20)

Primary citation

Zhou, J.,Liang, B.,Li, H.
Functional and Structural Impact of Target Uridine Substitutions on the H/ACA Ribonucleoprotein Particle Pseudouridine Synthase .
Biochemistry, 49:6276-6281, 2010

PubMed Abstract: Box H/ACA ribonucleoprotein protein particles catalyze the majority of pseudouridylation in functional RNA. Different from stand alone pseudouridine synthases, the RNP pseudouridine synthase comprises multiple protein subunits and an RNA subunit. Previous studies showed that each subunit, regardless its location, is sensitive to the step of subunit placement at the catalytic center and potentially to the reaction status of the substrate. Here we describe the impact of chemical substitutions of target uridine on enzyme activity and structure. We found that 3-methyluridine in place of uridine inhibited its isomerization while 2'-deoxyuridine or 4-thiouridine did not. Significantly, crystal structures of an archaeal box H/ACA RNP bound with the nonreactive and the two postreactive substrate analogues showed only subtle structural changes throughout the assembly except for a conserved tyrosine and a substrate anchoring loop of Cbf5. Our results suggest a potential role of these elements and the subunit that contacts them in substrate binding and product release.

PubMed: 20575532
DOI: 10.1021/bi1006699

Experimental method

X-RAY DIFFRACTION (2.678 Å)