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PDBsum entry 2gje
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Translation/RNA
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PDB id
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2gje
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References listed in PDB file
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Key reference
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Title
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Crystal structures of t. Brucei mrp1/mrp2 guide-Rna binding complex reveal RNA matchmaking mechanism.
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Authors
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M.A.Schumacher,
E.Karamooz,
A.Zíková,
L.Trantírek,
J.Lukes.
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Ref.
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Cell, 2006,
126,
701-711.
[DOI no: ]
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PubMed id
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Abstract
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The mitochondrial RNA binding proteins MRP1 and MRP2 form a heteromeric complex
that functions in kinetoplastid RNA editing. In this process, MRP1/MRP2 serves
as a matchmaker by binding to guide RNAs and facilitating their hybridization
with cognate preedited mRNAs. To understand the mechanism by which this complex
performs RNA matchmaking, we determined structures of Trypanosoma brucei
apoMRP1/MRP2 and an MRP1/MRP2-gRNA complex. The structures show that MRP1/MRP2
is a heterotetramer and, despite little sequence homology, each MRP subunit
exhibits the same "Whirly" transcription-factor fold. The gRNA
molecule binds to the highly basic beta sheet surface of the MRP complex via
nonspecific, electrostatic contacts. Strikingly, while the gRNA stem/loop II
base is anchored to the basic surface, stem/loop I (the anchor sequence) is
unfolded and its bases exposed to solvent. Thus, MRP1/MRP2 acts as an RNA
matchmaker by stabilizing the RNA molecule in an unfolded conformation suitable
for RNA-RNA hybridization.
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Figure 1.
Figure 1. Structure of the MRP1/MRP2 Complex
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Figure 2.
Figure 2. MRP1 and MRP2 Have “Whirly”
Transcription-Factor Folds and Form a Heterotetramer
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The above figures are
reprinted
by permission from Cell Press:
Cell
(2006,
126,
701-711)
copyright 2006.
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