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3 Structure Hits
1 Citation
26 Ligand Hits
Query Parameters:
Simple query for a list of PDB IDs (3 IDs) : 3NGY, 3NGZ, 3NH0
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Escherichia coli only (3)
Taxonomy
Bacteria only (3)
Experimental Method
X-RAY (3)
X-Ray Resolution
2.1 - 2.2 (1)
2.2 - 2.3 (1)
2.3 and more (1)
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Feb 2011 (3)
this year (3)
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Polymer Type
Mixed (2)
Protein (1)
Enzyme Classification
3.1.13: Exoribonucleases produc ... (3)
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Displaying results 1 - 3 of 3 total | Page 1 of 1 | Jump to page:
3NGY
Crystal structure of RNase T (E92G mutant)
Authors:
Hsiao, Y.-Y.
,
Yuan, H.S.
Release Date:
2011-02-16
Classification:
Hydrolase
Experiment:
X-RAY DIFFRACTION with resolution of 2.20 Å
Compound:
2 Polymers
[
Display Full Polymer Details
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Display for All Results
]
Molecule:
Ribonuclease T
Polymer:
1
Type:
polypeptide(L)
Length:
235
Chains:
A, B, C, D
EC#:
3.1.13.-
Mutation:
E92G
Molecule:
his tag sequence
Polymer:
2
Type:
polypeptide(L)
Length:
6
Chains:
E
1 Ligand
[
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]
Image
Identifier
Name
Formula
CO
COBALT (II) ION
Co
Citation:
Structural basis for RNA trimming by RNase T in stable RNA 3'-end maturation
(2011)
Nat.Chem.Biol.
PubMed Abstract:
RNA maturation relies on various exonucleases to remove nucleotides successively from the 5' or 3' end of nucleic acids. However, little is known regarding the molecular basis for substrate and cleavage preference of exonucleases. Our biochemical and structural analyses on RNase T-DNA complexes show that the RNase T dimer has an ideal architecture for binding a duplex with a short 3' overhang to produce a digestion product of a duplex with a 2-nucleotide (nt) or 1-nt 3' overhang, depending on the composition of the last base pair in the duplex. A 'C-filter' in RNase T screens out the nucleic acids with 3'-terminal cytosines for hydrolysis by inducing a disruptive conformational change at the active site. Our results reveal the general principles and the working mechanism for the final trimming step made by RNase T in the maturation of stable RNA and pave the way for the understanding of other DEDD family exonucleases.
Citation Authors:
Hsiao, Y.-Y.
,
Yang, C.-C.
,
Lin, C.L.
,
Lin, J.L.J.
,
Duh, Y.
,
Yuan, H.S.
[
Display Full Abstract
|
Display for All Results
]
3NGZ
Crystal structure of RNase T in complex with a non-preferred ssDNA (GC) with one Mg in the active site
Authors:
Hsiao, Y.-Y.
,
Yuan, H.S.
Release Date:
2011-02-16
Classification:
Hydrolase/dna
Experiment:
X-RAY DIFFRACTION with resolution of 2.10 Å
Compound:
2 Polymers
[
Display Full Polymer Details
|
Display for All Results
]
Molecule:
Ribonuclease T
Polymer:
1
Type:
polypeptide(L)
Length:
235
Chains:
A, B
EC#:
3.1.13.-
Mutation:
E92G
Molecule:
5'-D(P*GP*C)-3'
Polymer:
2
Type:
polydeoxyribonucleotide
Length:
2
Chains:
C, D
Other Details:
ssDNA
2 Ligands
[
Display Full Ligand Details
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Display for All Results
]
Image
Identifier
Name
Formula
CO
COBALT (II) ION
Co
MG
MAGNESIUM ION
Mg
Citation:
Structural basis for RNA trimming by RNase T in stable RNA 3'-end maturation
(2011)
Nat.Chem.Biol.
PubMed Abstract:
RNA maturation relies on various exonucleases to remove nucleotides successively from the 5' or 3' end of nucleic acids. However, little is known regarding the molecular basis for substrate and cleavage preference of exonucleases. Our biochemical and structural analyses on RNase T-DNA complexes show that the RNase T dimer has an ideal architecture for binding a duplex with a short 3' overhang to produce a digestion product of a duplex with a 2-nucleotide (nt) or 1-nt 3' overhang, depending on the composition of the last base pair in the duplex. A 'C-filter' in RNase T screens out the nucleic acids with 3'-terminal cytosines for hydrolysis by inducing a disruptive conformational change at the active site. Our results reveal the general principles and the working mechanism for the final trimming step made by RNase T in the maturation of stable RNA and pave the way for the understanding of other DEDD family exonucleases.
Citation Authors:
Hsiao, Y.-Y.
,
Yang, C.-C.
,
Lin, C.L.
,
Lin, J.L.J.
,
Duh, Y.
,
Yuan, H.S.
[
Display Full Abstract
|
Display for All Results
]
3NH0
Crystal structure of RNase T in complex with a non-preferred ssDNA (AAC)
Authors:
Hsiao, Y.-Y.
,
Yuan, H.S.
Release Date:
2011-02-16
Classification:
Hydrolase/dna
Experiment:
X-RAY DIFFRACTION with resolution of 2.30 Å
Compound:
2 Polymers
[
Display Full Polymer Details
|
Display for All Results
]
Molecule:
Ribonuclease T
Polymer:
1
Type:
polypeptide(L)
Length:
235
Chains:
A, B
EC#:
3.1.13.-
Molecule:
5'-D(*TP*TP*AP*CP*AP*AP*C)-3'
Polymer:
2
Type:
polydeoxyribonucleotide
Length:
7
Chains:
C, D
Other Details:
ssDNA
Citation:
Structural basis for RNA trimming by RNase T in stable RNA 3'-end maturation
(2011)
Nat.Chem.Biol.
PubMed Abstract:
RNA maturation relies on various exonucleases to remove nucleotides successively from the 5' or 3' end of nucleic acids. However, little is known regarding the molecular basis for substrate and cleavage preference of exonucleases. Our biochemical and structural analyses on RNase T-DNA complexes show that the RNase T dimer has an ideal architecture for binding a duplex with a short 3' overhang to produce a digestion product of a duplex with a 2-nucleotide (nt) or 1-nt 3' overhang, depending on the composition of the last base pair in the duplex. A 'C-filter' in RNase T screens out the nucleic acids with 3'-terminal cytosines for hydrolysis by inducing a disruptive conformational change at the active site. Our results reveal the general principles and the working mechanism for the final trimming step made by RNase T in the maturation of stable RNA and pave the way for the understanding of other DEDD family exonucleases.
Citation Authors:
Hsiao, Y.-Y.
,
Yang, C.-C.
,
Lin, C.L.
,
Lin, J.L.J.
,
Duh, Y.
,
Yuan, H.S.
[
Display Full Abstract
|
Display for All Results
]
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