5FIR

Crystal structure of C. elegans XRN2 in complex with the XRN2-binding domain of PAXT-1

Summary for 5FIR

• Entry DOI: 10.2210/pdb5fir/pdb
• Descriptor: 5'-3' EXORIBONUCLEASE 2 HOMOLOG, PAXT-1, SULFATE ION, ... (4 entities in total)
• Functional Keywords: hydrolase, 5'-3' exoribonuclease, mirna turnover
• Biological source: CAENORHABDITIS ELEGANS; More
• Cellular location: Nucleus : Q9U299
• Total number of polymer chains: 12
• Total formula weight: 505981.41

Authors

Richter, H.,Katic, I.,Gut, H.,Grosshans, H. (deposition date: 2015-10-02, release date: 2016-01-20, Last modification date: 2024-11-20)

Primary citation

Richter, H.,Katic, I.,Gut, H.,Grosshans, H.
Structural Basis and Function of Xrn2-Binding by Xtb Domains
Nat.Struct.Mol.Biol., 23:164-, 2016

PubMed Abstract: The RNase XRN2 is essential in RNA metabolism. In Caenorhabditis elegans, XRN2 functions with PAXT-1, which shares a putative XRN2-binding domain (XTBD) with otherwise unrelated mammalian proteins. Here, we characterize the structure and function of an XTBD-XRN2 complex. Although XTBD stably interconnects two XRN2 domains through numerous interacting residues, mutation of a single critical residue suffices to disrupt XTBD-XRN2 complexes in vitro and to recapitulate paxt-1-null mutant phenotypes in vivo. Demonstrating conservation of function, vertebrate XTBD-containing proteins bind XRN2 in vitro, and human CDKN2AIPNL (HsC2AIL) can substitute for PAXT-1 in vivo. In vertebrates, which express three distinct XTBD-containing proteins, XRN2 may partition into distinct stable heterodimeric complexes, which probably differ in subcellular localization or function. In C. elegans, complex formation with PAXT-1, the sole XTBD protein, serves to preserve the stability of XRN2 in the absence of substrate.

PubMed: 26779609
DOI: 10.1038/NSMB.3155

Experimental method

X-RAY DIFFRACTION (2.836 Å)