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4WZR

Crystal structure of human Puf-A

Summary for 4WZR
Entry DOI10.2210/pdb4wzr/pdb
DescriptorPumilio domain-containing protein KIAA0020, GLYCEROL (3 entities in total)
Functional Keywordspumilio repeat protein, rna binding protein
Biological sourceHomo sapiens (Human)
Total number of polymer chains2
Total formula weight119512.87
Authors
Qiu, C.,Hall, T.M.T. (deposition date: 2014-11-20, release date: 2014-12-31, Last modification date: 2024-02-28)
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 (2.154 Å)
Structure validation

237735

数据于2025-06-18公开中

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