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PDBsum entry 1aqz
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Insights into specificity of cleavage and mechanism of cell entry from the crystal structure of the highly specific aspergillus ribotoxin, Restrictocin.
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Authors
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X.Yang,
K.Moffat.
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Ref.
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Structure, 1996,
4,
837-852.
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PubMed id
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Abstract
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BACKGROUND: Restriction, a highly specific ribotoxin made by the fungus
Aspergillus restrictus, cleaves a single phosphodiester bond in the 28S RNA of
eukaryotic ribosomes, inhibiting protein synthesis. The sequence around this
cleavage site is a binding site for elongation factors, and is conserved in all
cytoplasmic ribosomes. The catalytic mechanism of restrictocin and the reasons
for its high substrate specificity are unknown. No structure has been determined
for any other member of the Aspergillus ribotoxin family. RESULTS: The crystal
structure of restrictocin was determined at 2.1 A resolution by single
isomorphous replacement and anomalous scattering techniques, and refined to 1.7
A resolution using synchrotron Laue data. The structural core of the protein, in
which a three-turn alpha helix is packed against a five-stranded antiparallel
beta sheet, can be well aligned with that of ribonuclease T1. Large positively
charged peripheral loops near the active site construct a platform with a
concave surface for RNA binding. CONCLUSIONS: Restriction appears to combine the
catalytic components of T1 ribonucleases with the base recognition components of
Sa ribonucleases. Modeling studies using an NMR structure of an RNA substrate
analog suggest that the tertiary structure of the substrate RNA is important in
protein-RNA recognition, fitting closely into the concavity of the presumed
binding site. We speculate that the large 39-residue loop L3, which has
similarities to loops found in lectin sugar-binding domains, may be responsible
for restrictocin's ability to cross cell membranes.
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Added reference #1*
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Title
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Structure refinement against synchrotron Laue data: strategies for data collection and reduction.
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Authors
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X.Yang,
Z.Ren,
K.Moffat.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1998,
54,
367-377.
[DOI no: ]
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PubMed id
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Figure 2.
Figure 2
Completeness versus resolution. Data points are located at the high-resolution side of
each bin. (a) Singles, deconvoluted multiples and those combined for data set Laue62; (b)
data sets Laue31-1, Laue31-2 and Laue62.
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Figure 5.
Figure 5
The Luzzati plot of the restrictocin model refined against data set Laue62. Data points
are located at the high-resolution side of each bin.
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The above figures are
reproduced from the cited reference
with permission from the IUCr
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*Note, "added" references are those not in the PDB file but
which have either been obtained from the journal or suggested by the
author(s).
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Secondary reference #1
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Title
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The conformation of the sarcin/ricin loop from 28s ribosomal RNA.
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Authors
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A.A.Szewczak,
P.B.Moore,
Y.L.Chang,
I.G.Wool.
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Ref.
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Proc Natl Acad Sci U S A, 1993,
90,
9581-9585.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Determination and restrained least-Squares refinement of the structures of ribonuclease sa and its complex with 3'-Guanylic acid at 1.8 a resolution.
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Authors
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J.Sevcik,
E.J.Dodson,
G.G.Dodson.
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Ref.
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Acta Crystallogr B, 1991,
47,
240-253.
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PubMed id
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Secondary reference #3
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Title
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Crystallization and preliminary characterization of mitogillin, A ribosomal ribonuclease from aspergillus restrictus.
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Authors
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S.E.Martinez,
J.L.Smith.
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Ref.
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J Mol Biol, 1991,
218,
489-492.
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PubMed id
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Secondary reference #4
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Title
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The mechanism of action of the cytotoxic nuclease alpha-Sarcin and its use to analyse ribosome structure
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Author
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I.G.Wool.
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Ref.
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trends biochem sci, 1984,
9,
14.
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Secondary reference #5
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Title
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Specific protein-Nucleic acid recognition in ribonuclease t1-2'-Guanylic acid complex: an x-Ray study.
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Authors
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U.Heinemann,
W.Saenger.
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Ref.
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Nature, 1982,
299,
27-31.
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PubMed id
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