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3K49

Puf3 RNA binding domain bound to Cox17 RNA 3' UTR recognition sequence site B

Summary for 3K49
Entry DOI10.2210/pdb3k49/pdb
Related3K4E
DescriptormRNA-binding protein PUF3, RNA (5'-R(*CP*CP*UP*GP*UP*AP*AP*AP*UP*A)-3'), CITRIC ACID, ... (4 entities in total)
Functional Keywordspuf3, pumilio, rna binding, mitochondrial mrna, membrane, mitochondrion, mitochondrion outer membrane, phosphoprotein, rna-binding, rna binding protein - rna complex, rna binding protein / rna
Biological sourceSaccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
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Cellular locationMitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side: Q07807
Total number of polymer chains6
Total formula weight137019.53
Authors
Zhu, D.,Stumpf, C.R.,Krahn, J.M.,Wickens, M.,Hall, T.M.T. (deposition date: 2009-10-05, release date: 2009-10-27, Last modification date: 2023-09-06)
Primary citationZhu, D.,Stumpf, C.R.,Krahn, J.M.,Wickens, M.,Hall, T.M.
A 5' cytosine binding pocket in Puf3p specifies regulation of mitochondrial mRNAs.
Proc.Natl.Acad.Sci.USA, 106:20192-20197, 2009
Cited by
PubMed Abstract: A single regulatory protein can control the fate of many mRNAs with related functions. The Puf3 protein of Saccharomyces cerevisiae is exemplary, as it binds and regulates more than 100 mRNAs that encode proteins with mitochondrial function. Here we elucidate the structural basis of that specificity. To do so, we explore the crystal structures of Puf3p complexes with 2 cognate RNAs. The key determinant of Puf3p specificity is an unusual interaction between a distinctive pocket of the protein with an RNA base outside the "core" PUF-binding site. That interaction dramatically affects binding affinity in vitro and is required for regulation in vivo. The Puf3p structures, combined with those of Puf4p in the same organism, illuminate the structural basis of natural PUF-RNA networks. Yeast Puf3p binds its own RNAs because they possess a -2C and is excluded from those of Puf4p which contain an additional nucleotide in the core-binding site.
PubMed: 19918084
DOI: 10.1073/pnas.0812079106
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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