Crystallization and X‐ray diffraction analysis of the Trp/amber editing site of hepatitis delta virus (+)RNA: a case of rational design
Identifieur interne : 003007 ( Main/Exploration ); précédent : 003006; suivant : 003008Crystallization and X‐ray diffraction analysis of the Trp/amber editing site of hepatitis delta virus (+)RNA: a case of rational design
Auteurs : Celeste Macelrevey [États-Unis] ; Joseph E. Wedekind [États-Unis]Source :
- Acta Crystallographica Section F [ 1744-3091 ] ; 2005-12.
English descriptors
- Teeft :
- Acta, Acta cryst, Ammonium sulfate, Asymmetric unit, Cryst, Crystal growth, Crystallization, Crystals diffracted, Data collection, Diffracted, Diffraction data, Diffraction experiments, Duplex, Editing site, Glycerol, Hampton research, Hepatitis delta virus, High symmetry, Internal loops, Macelrevey wedekind editing site, Macroseeding experiments, Magnesium chloride, Methods enzymol, Minimal substrate, Molecular replacement, Native sequence, Natl acad, Open reading frame, Potassium acetate, Small crystals, Sodium cacodylate, Sodium cacodylate buffer, Solvent content, Space group, Structure determination, Synthetic mother liquor, Trigonal habit, Twinning, Unedited, Wedekind, Wedekind mckay.
Abstract
RNA editing by mammalian ADAR1 (Adenosine Deaminase Acting on RNA) is required for the life cycle of the hepatitis delta virus (HDV). Editing extends the single viral open reading frame to yield two protein products of alternate length. ADARs are believed to recognize double‐stranded RNA substrates via a `structure‐based' readout mechanism. Crystals of 10‐mer duplexes representing the HDV RNA‐editing site diffracted to 1.35 Å resolution, but suffered from merohedral twinning and averaging of the base registry. Expansion of the construct to include two flanking 3 × 1 internal loops yielded crystals in the primitive tetragonal space group P41212 or P43212. X‐ray diffraction data were collected to 2.8 Å resolution, revealing a unit cell with parameters a = 62.5, c = 63.5 Å. The crystallization and X‐ray analysis of multiple forms of the HDV RNA‐editing substrate, encounters with common RNA crystal‐growth defects and a strategy to overcome these problems are reported.
Url:
DOI: 10.1107/S1744309105035888
Affiliations:
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Wedekind</name><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642</wicri:regionArea><wicri:noRegion>New York 14642</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Acta Crystallographica Section F</title><title level="j" type="alt">ACTA CRYSTALLOGRAPHICA F</title><idno type="ISSN">1744-3091</idno><idno type="eISSN">1744-3091</idno><imprint><biblScope unit="vol">61</biblScope><biblScope unit="issue">12</biblScope><biblScope unit="page" from="1049">1049</biblScope><biblScope unit="page" to="1053">1053</biblScope><publisher>Munksgaard International Publishers</publisher><pubPlace>5 Abbey Square, Chester, Cheshire CH1 2HU, England</pubPlace><date type="published" when="2005-12">2005-12</date></imprint><idno type="ISSN">1744-3091</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">1744-3091</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acta</term><term>Acta cryst</term><term>Ammonium sulfate</term><term>Asymmetric unit</term><term>Cryst</term><term>Crystal growth</term><term>Crystallization</term><term>Crystals diffracted</term><term>Data collection</term><term>Diffracted</term><term>Diffraction data</term><term>Diffraction experiments</term><term>Duplex</term><term>Editing site</term><term>Glycerol</term><term>Hampton research</term><term>Hepatitis delta virus</term><term>High symmetry</term><term>Internal loops</term><term>Macelrevey wedekind editing site</term><term>Macroseeding experiments</term><term>Magnesium chloride</term><term>Methods enzymol</term><term>Minimal substrate</term><term>Molecular replacement</term><term>Native sequence</term><term>Natl acad</term><term>Open reading frame</term><term>Potassium acetate</term><term>Small crystals</term><term>Sodium cacodylate</term><term>Sodium cacodylate buffer</term><term>Solvent content</term><term>Space group</term><term>Structure determination</term><term>Synthetic mother liquor</term><term>Trigonal habit</term><term>Twinning</term><term>Unedited</term><term>Wedekind</term><term>Wedekind mckay</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">RNA editing by mammalian ADAR1 (Adenosine Deaminase Acting on RNA) is required for the life cycle of the hepatitis delta virus (HDV). Editing extends the single viral open reading frame to yield two protein products of alternate length. ADARs are believed to recognize double‐stranded RNA substrates via a `structure‐based' readout mechanism. Crystals of 10‐mer duplexes representing the HDV RNA‐editing site diffracted to 1.35 Å resolution, but suffered from merohedral twinning and averaging of the base registry. Expansion of the construct to include two flanking 3 × 1 internal loops yielded crystals in the primitive tetragonal space group P41212 or P43212. X‐ray diffraction data were collected to 2.8 Å resolution, revealing a unit cell with parameters a = 62.5, c = 63.5 Å. The crystallization and X‐ray analysis of multiple forms of the HDV RNA‐editing substrate, encounters with common RNA crystal‐growth defects and a strategy to overcome these problems are reported.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Macelrevey, Celeste" sort="Macelrevey, Celeste" uniqKey="Macelrevey C" first="Celeste" last="Macelrevey">Celeste Macelrevey</name></noRegion><name sortKey="Wedekind, Joseph E" sort="Wedekind, Joseph E" uniqKey="Wedekind J" first="Joseph E." last="Wedekind">Joseph E. Wedekind</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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