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PDBsum entry 4j0w
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RNA binding protein
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PDB id
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4j0w
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PDB id:
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| Name: |
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RNA binding protein
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Title:
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Structure of u3-55k
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Structure:
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U3 small nucleolar RNA-interacting protein 2. Chain: a. Fragment: wd domain, unp residues 137-475. Synonym: rrp9 homolog, u3 small nucleolar ribonucleoprotein- associated 55 kda protein, u3 snornp-associated 55 kda protein, u3- 55k. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: rrp9, rnu3ip2, u355k. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: high five.
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Resolution:
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1.70Å
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R-factor:
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0.211
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R-free:
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0.232
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Authors:
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L.Zhang,J.Lin,K.Ye
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Key ref:
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L.Zhang
et al.
(2013).
Structural and functional analysis of the U3 snoRNA binding protein Rrp9.
RNA,
19,
701-711.
PubMed id:
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Date:
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31-Jan-13
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Release date:
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05-Jun-13
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PROCHECK
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Headers
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References
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O43818
(U3IP2_HUMAN) -
U3 small nucleolar RNA-interacting protein 2 from Homo sapiens
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Seq:
Struc:
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475 a.a.
327 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 3 residue positions (black
crosses)
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RNA
19:701-711
(2013)
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PubMed id:
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Structural and functional analysis of the U3 snoRNA binding protein Rrp9.
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L.Zhang,
J.Lin,
K.Ye.
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ABSTRACT
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The U3 snoRNA is required for 18S rRNA processing and small subunit ribosome
formation in eukaryotes. Different from other box C/D snoRNAs, U3 contains an
extra 5' domain that pairs with pre-rRNA and a unique B/C motif essential for
recruitment of the U3-specific Rrp9 protein. Here, we analyze the structure and
function of Rrp9 with crystallographic, biochemical, and cellular approaches.
Rrp9 is composed of a WD repeat domain and an N-terminal region. The crystal
structures of the WD domain of yeast Rrp9 and its human ortholog U3-55K were
determined, revealing a typical seven-bladed propeller fold. Several conserved
surface patches on the WD domain were identified, and their function in RNP
assembly and yeast growth were analyzed by mutagenesis. Prior association of
Snu13 with the B/C motif was found to enhance the specific binding of the WD
domain. We show that a conserved 7bc loop is crucial for specific recognition of
U3, nucleolar localization of Rrp9, and yeast growth. In addition, we show that
the N-terminal region of Rrp9 contains a bipartite nuclear localization signal
that is dispensable for nucleolar localization. Our results provide insight into
the functional sites of Rrp9.
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Links
