4oe1
From Proteopedia
Crystal structure of the pentatricopeptide repeat protein PPR10 (C256S/C430S/C449S) in complex with an 18-nt PSAJ rna element
Structural highlights
FunctionPPR10_MAIZE Involved in chloroplast mRNA stability (PubMed:19424177, PubMed:21173259, PubMed:22156165). Binds specifically to two intergenic RNA regions of similar sequence located in the chloroplast atpH 5'-UTR and psaJ 3'-UTR, and serves as a barrier to RNA decay (PubMed:19424177). Binding to a specific site in the intergenic region of the chloroplast atpH is sufficient to block 5'-3' and 3'-5' exonucleases (PubMed:21173259). Acts as protein barrier to block mRNA degradation by exonucleases, and defines processed mRNA termini in chloroplasts (PubMed:22156165). Remodels the structure of the atpH ribosome-binding site in a manner that can account for its ability to enhance translation (PubMed:21173259). Stabilizes a RNA 3'-end downstream from psaI (PubMed:30125002). Binds atpH RNA as a monomer (PubMed:25609698).[1] [2] [3] [4] [5] Publication Abstract from PubMedPentatricopeptide repeat (PPR) proteins, particularly abundant in plastids and mitochrondria of angiosperms, include a large number of sequence-specific RNA binding proteins which are involved indiverse aspects of organelle RNA metabolisms. PPR proteins contain multiple tandom repeats and each repeat can specifically recognize a RNA base through residues 2, 5, and 35 in a modular fashion. The crystal structure of PPR10 from maize chloroplast exhibits dimeric existence both in the absence and presence of the 18-nucleotide (nt) psaJ RNA element. However, previous biochemical analysis suggested a monomeric shift of PPR10 upon RNA binding. In this report, we show that the amino-ternimal segments of PPR10 determine the dimerization state of PPR10. A single amino acid alteration of cysteine to serine within repeat 10 of PPR10 further drives dimerization of PPR10. The biochemical elucidation of the determinants for PPR10 dimerization may provide an important foundation to understand the working mechanisms of PPR proteins underlying their diverse physiological functions. Examination of the Dimerization States of the Single-stranded RNA-recognition Protein PPR10.,Li Q, Yan C, Xu H, Wang Z, Long J, Li W, Wu J, Yin P, Yan N J Biol Chem. 2014 Sep 17. pii: jbc.M114.575472. PMID:25231995[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Large Structures | Zea mays | Li Q | Wu J | Yan C | Yan N | Yin P
