2v9k

From Proteopedia

Revision as of 10:41, 23 January 2008

CRYSTAL STRUCTURE OF HUMAN PUS10, A NOVEL PSEUDOURIDINE SYNTHASE.

Overview

Pseudouridine (Psi) synthases catalyze the formation of one or more, specific Psis in structured RNAs. Five families of Psi synthases have been, characterized based on sequence homology. Pus10 has no significant, sequence homology to these defined families and therefore represents a new, family of Psi synthases. Initial characterization studies show that an, archael Pus10 catalyzes the universally conserved Psi55 in tRNA. We, present here the crystal structure of human Pus10 at 2.0 A resolution, which is the first structural description from this novel Psi synthase, family. Pus10 is a crescent-shaped molecule with two domains, the, universally conserved Psi synthase catalytic domain and a THUMP-containing, domain, which is unique to the Pus10 family. Superposition of the, catalytic domains of Pus10 and other Psi synthases identifies the full set, of conserved Psi synthase active site residues indicating that Pus10, likely employs a similar catalytic mechanism to other Psi synthases. The, Pus10 active site is located in a deep pocket of a basic cleft adjacent to, flexible thumb and forefinger loops, which could provide further, stabilization for binding the RNA substrate. Modeling studies demonstrate, that the cleft between the catalytic and accessory domain is large enough, and electrostatically compatible to accommodate an RNA stem and support, the role of the N-terminal domain as an accessory RNA-binding domain.

About this Structure

2V9K is a Single protein structure of sequence from Homo sapiens with , , and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Crystal Structure of Human Pus10, A Novel Pseudouridine Synthase., McCleverty CJ, Hornsby M, Spraggon G, Kreusch A, J Mol Biol. 2007 Aug 29;. PMID:17900615

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