3PQV

Cyclase homolog

Summary for 3PQV

• Entry DOI: 10.2210/pdb3pqv/pdb
• Descriptor: Rcl1 protein, D(-)-TARTARIC ACID, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• Functional Keywords: rtc-like, cyclase-like, modular, alpha-beta, anion pocket, ribosome biogenesis, unknown function
• Biological source: Kluyveromyces lactis (Yeast)
• Total number of polymer chains: 4
• Total formula weight: 161447.75

Authors

Tanaka, N.,Smith, P.,Shuman, S. (deposition date: 2010-11-27, release date: 2011-04-13, Last modification date: 2024-02-21)

Primary citation

Tanaka, N.,Smith, P.,Shuman, S.
Crystal structure of Rcl1, an essential component of the eukaryal pre-rRNA processosome implicated in 18s rRNA biogenesis.
Rna, 17:595-602, 2011

PubMed Abstract: Rcl1 is an essential nucleolar protein required for U3 snoRNA-guided pre-rRNA processing at sites flanking the 18S rRNA sequence. A potential catalytic role for Rcl1 during pre-rRNA cleavage has been suggested based on its primary structure similarity to RNA 3'-terminal phosphate cyclase (Rtc) enzymes, which perform nucleotidyl transfer and phosphoryl transfer reactions at RNA ends. Here, we report the 2.6 Å crystal structure of a biologically active yeast Rcl1, which illuminates its modular 4-domain architecture and overall homology with RNA cyclases while revealing numerous local differences that account for why Rtcs possess metal-dependent adenylyltransferase activity and Rcls do not. A conserved oxyanion-binding site in Rcl1 was highlighted for possible catalytic or RNA-binding functions. However, the benign effects of mutations in and around the anion site on Rcl1 activity in vivo militate against such a role.

PubMed: 21367972
DOI: 10.1261/rna.2571811

Experimental method

X-RAY DIFFRACTION (2.609 Å)