Structure of the C-terminal domain of the DEAD-box protein Dbp5 (3gfp)
(see also Helicase)
Publication Abstract from PubMed
The DExD/H-box RNA-dependent ATPase Dbp5 plays an essential role in the nuclear export of mRNA. Dbp5 localizes to the nuclear pore complex, where its ATPase activity is stimulated by Gle1 and its coactivator inositol hexakisphosphate. Here, we present the crystal structure of the C-terminal domain of Dbp5, refined to 1.8 A. The structure reveals a RecA-like fold that contains two defining characteristics not present in other structurally characterized DExD/H-box proteins: a C-terminal alpha-helix and a loop connecting beta5 and alpha4, both of which are composed of conserved and unique elements in the Dbp5 primary sequence. Using structure-guided mutagenesis, we have identified several charged surface residues that, when mutated, weaken the binding of Gle1 and inhibit the ability of Gle1 to stimulate Dbp5's ATPase activity. In vivo analysis of the same mutations reveals that those mutants displaying the weakest ATPase stimulation in vitro are also unable to support yeast growth. Analysis of the correlation between the in vitro and in vivo data indicates that a threshold level of Dbp5 ATPase activity is required for cellular mRNA export that is not met by the unstimulated enzyme, suggesting a possible mechanism by which Dbp5's activity can be modulated to regulate mRNA export.
Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1., Dossani ZY, Weirich CS, Erzberger JP, Berger JM, Weis K, Proc Natl Acad Sci U S A. 2009 Sep 22;106(38):16251-6. Epub 2009 Sep 2. PMID:19805289
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
3GFP is a 1 chain structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
The C-terminal domain of Dbp5 is a RecA-like fold, displayed here similar to figure 1A of the paper describing the structure:
- of the C-terminal domain of Dbp5. .
- .
to see if they affect interaction with Gle1. See figure 2C of the paper describing the structure.
that are not present in the corresponding domain of other structurally characterized DExD/H-box proteins: an extended loop element after strand β5 and a conserved α-helix at its C-terminus, both shown in red.
Reference
- Dossani ZY, Weirich CS, Erzberger JP, Berger JM, Weis K. Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1. Proc Natl Acad Sci U S A. 2009 Sep 22;106(38):16251-6. Epub 2009 Sep 2. PMID:19805289
Content Donators
Created with the participation of Eran Hodis, Wayne Decatur.
