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PDBsum entry 5co0
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Transcription/DNA
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PDB id
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5co0
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PDB id:
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| Name: |
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Transcription/DNA
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Title:
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Crystal structure of the mterf1 y288a substitution bound to the termination sequence.
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Structure:
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Transcription termination factor 1, mitochondrial. Chain: o. Synonym: cdna flj51270,highly similar to transcription termination factor,mitochondrial. Engineered: yes. Mutation: yes. DNA (5'- d( Ap Tp Tp Ap Cp Cp Gp Gp Gp Cp Tp Cp Tp Gp Cp Cp Ap Tp Cp Tp Tp A)- 3').
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: mterf1. Expressed in: escherichia coli. Expression_system_taxid: 469008. Synthetic: yes. Organism_taxid: 9606
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Resolution:
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2.65Å
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R-factor:
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0.209
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R-free:
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0.264
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Authors:
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J.Byrnes,K.Hauser,L.Norona,E.Mejia,C.Simmerling,M.Garcia-Diaz
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Key ref:
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J.Byrnes
et al.
(2016).
Base Flipping by MTERF1 Can Accommodate Multiple Conformations and Occurs in a Stepwise Fashion.
J Mol Biol,
428,
2542-2556.
PubMed id:
DOI:
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Date:
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18-Jul-15
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Release date:
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25-Nov-15
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PROCHECK
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Headers
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References
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Q99551
(MTEF1_HUMAN) -
Transcription termination factor 1, mitochondrial from Homo sapiens
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Seq:
Struc:
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399 a.a.
324 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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A-T-T-A-C-C-G-G-G-C-T-C-T-G-C-C-A-T-C-T-T-A
22 bases
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T-A-A-G-A-T-G-G-C-A-G-A-G-C-C-C-G-G-T-A-A-T
22 bases
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DOI no:
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J Mol Biol
428:2542-2556
(2016)
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PubMed id:
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Base Flipping by MTERF1 Can Accommodate Multiple Conformations and Occurs in a Stepwise Fashion.
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J.Byrnes,
K.Hauser,
L.Norona,
E.Mejia,
C.Simmerling,
M.Garcia-Diaz.
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ABSTRACT
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Human mitochondrial transcription termination occurs within the leu-tRNA gene
and is mediated by the DNA binding protein MTERF1. The crystal structure of
MTERF1 bound to the canonical termination sequence reveals a rare base flipping
event that involves the eversion of three nucleotides. These nucleotides are
stabilized by stacking interactions with three MTERF1 residues, which are
essential not only for base flipping but also for termination activity. To
further understand the mechanism of base flipping, we examined each of the
individual stacking interactions in structural, energetic and functional detail.
Individual substitutions of Arg162, Tyr288 and Phe243 have revealed unequal
contributions to overall termination activity. Furthermore, our work identifies
an important role for Phe322 in the base flipping mechanism and we demonstrate
how Phe322 and Phe243 are important for coupling base flipping between the heavy
and light strand DNA chains. We propose a stepwise model for the base flipping
process that recapitulates our observations. Finally, we show that MTERF1 has
the ability to accommodate alternate active conformations. The adaptability of
base flipping has implications for MTERF1 function and for the putative function
of MTERF1 at alternative binding sites in human mitochondria.
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Links
