2dyd
From Proteopedia
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Solution structure of the PABC domain from Triticum aevestium poly(A)-binding protein
Overview
In animals, the PABC domain from poly (A)-binding protein recruits, proteins containing a specific interacting motif (PAM-2) to the mRNP, complex. These proteins include Paip1, Paip2, and eukaryotic release, factor 3 (eRF3), all of which regulate PABP function in translation. The, following reports the solution structure of PABC from Triticum avestium, (wheat) poly (A)-binding protein determined by NMR spectroscopy. Wheat, PABC (wPABC) is an alpha-helical protein domain, which displays a fold, highly similar to the human PABC domain and contains a PAM-2 peptide, binding site. Through a bioinformatics search, several plant proteins, containing a PAM-2 site were identified including the early response to, dehydration protein (ERD-15), which was previously shown to regulate, PABP-dependent translation. The plant PAM-2 proteins contain a variety of, conserved sequences including a PABP-interacting 1 motif (PAM-1), RNA, binding domains, an SMR endonuclease domain, and a poly (A)-nuclease, regulatory domain, all of which suggest a function in either translation, or mRNA metabolism. The proteins identified are well conserved throughout, plant species but have no sequence homologues in metazoans. We show that, wPABC binds to the plant PAM-2 motif with high affinity through a, conserved mechanism. Overall, our results suggest that plant species have, evolved a distinct regulatory mechanism involving novel PABP binding, partners.
About this Structure
2DYD is a Single protein structure of sequence from Triticum aestivum. Full crystallographic information is available from OCA.
Reference
Solution structure of the PABC domain from wheat poly (A)-binding protein: an insight into RNA metabolic and translational control in plants., Siddiqui N, Osborne MJ, Gallie DR, Gehring K, Biochemistry. 2007 Apr 10;46(14):4221-31. Epub 2007 Mar 15. PMID:17358048
Page seeded by OCA on Wed Jan 23 15:10:46 2008
