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4WZW

Crystal structure of human Puf-A in complex with DNA

Summary for 4WZW
Entry DOI10.2210/pdb4wzw/pdb
Related4WZR
DescriptorPumilio domain-containing protein KIAA0020, DNA (5'-D(P*GP*GP*GP*GP*GP*GP*GP*GP*GP*GP*GP*GP*GP*G)-3'), DNA (5'-D(P*CP*CP*CP*CP*CP*CP*CP*CP*CP*CP*CP*CP*CP*CP*CP*C)-3') (3 entities in total)
Functional Keywordspumilio repeat protein, dna binding protein, rna binding protein-dna complex, rna binding protein/dna
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains3
Total formula weight68195.55
Authors
Qiu, C.,Hall, T.M.T. (deposition date: 2014-11-20, release date: 2014-12-31, Last modification date: 2023-09-27)
Primary citationQiu, C.,McCann, K.L.,Wine, R.N.,Baserga, S.J.,Hall, T.M.
A divergent Pumilio repeat protein family for pre-rRNA processing and mRNA localization.
Proc.Natl.Acad.Sci.USA, 111:18554-18559, 2014
Cited by
PubMed Abstract: Pumilio/feminization of XX and XO animals (fem)-3 mRNA-binding factor (PUF) proteins bind sequence specifically to mRNA targets using a single-stranded RNA-binding domain comprising eight Pumilio (PUM) repeats. PUM repeats have now been identified in proteins that function in pre-rRNA processing, including human Puf-A and yeast Puf6. This is a role not previously ascribed to PUF proteins. Here we present crystal structures of human Puf-A that reveal a class of nucleic acid-binding proteins with 11 PUM repeats arranged in an "L"-like shape. In contrast to classical PUF proteins, Puf-A forms sequence-independent interactions with DNA or RNA, mediated by conserved basic residues. We demonstrate that equivalent basic residues in yeast Puf6 are important for RNA binding, pre-rRNA processing, and mRNA localization. Thus, PUM repeats can be assembled into alternative folds that bind to structured nucleic acids in addition to forming canonical eight-repeat crescent-shaped RNA-binding domains found in classical PUF proteins.
PubMed: 25512524
DOI: 10.1073/pnas.1407634112
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9516 Å)
Structure validation

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