1MP1

Solution structure of the PWI motif from SRm160

Summary for 1MP1

• Entry DOI: 10.2210/pdb1mp1/pdb
• NMR Information: BMRB: 5162
• Descriptor: Ser/Arg-related nuclear matrix protein (1 entity in total)
• Functional Keywords: four helix bundle, rna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus matrix: Q8IYB3
• Total number of polymer chains: 1
• Total formula weight: 12869.05

Authors

Szymczyna, B.R.,Bowman, J.,McCracken, S.,Pineda-Lucena, A.,Lu, Y.,Cox, B.,Lambermon, M.,Graveley, B.R.,Arrowsmith, C.H.,Blencowe, B.J. (deposition date: 2002-09-11, release date: 2003-09-16, Last modification date: 2024-05-22)

Primary citation

Szymczyna, B.R.,Bowman, J.,McCracken, S.,Pineda-Lucena, A.,Lu, Y.,Cox, B.,Lambermon, M.,Graveley, B.R.,Arrowsmith, C.H.,Blencowe, B.J.
Structure and function of the PWI motif: a novel nucleic acid-binding domain that facilitates pre-mRNA processing.
Genes Dev., 17:461-475, 2003

PubMed Abstract: The PWI motif is a highly conserved domain of unknown function in the SRm160 splicing and 3'-end cleavage-stimulatory factor, as well as in several other known or putative pre-mRNA processing components. We show here that the PWI motif is a new type of RNA/DNA-binding domain that has an equal preference for single- and double-stranded nucleic acids. Deletion of the motif prevents SRm160 from binding RNA and stimulating 3'-end cleavage, and its substitution with a heterologous RNA-binding domain restores these functions. The NMR solution structure of the SRm160-PWI motif reveals a novel, four-helix bundle and represents the first example of an alpha-helical fold that can bind single-stranded (ss)RNA. Structure-guided mutagenesis indicates that the same surface is involved in RNA and DNA binding and requires the cooperative action of a highly conserved, adjacent basic region. Thus, the PWI motif is a novel type of nucleic acid-binding domain that likely has multiple important functions in pre-mRNA processing, including SRm160-dependent stimulation of 3'-end formation.

PubMed: 12600940
DOI: 10.1101/gad.1060403

Experimental method

SOLUTION NMR