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Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNA-dependent RNA polymerase.

Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNA-dependent RNA polymerase. Research Abstract Details 

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  • Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNA-dependent RNA polymerase. Abstract Text:

    laura l marcotteLaura L Marcotte,amanda b wassAmanda B Wass,david w goharaDavid W Gohara,harsh b pathakHarsh B Pathak,jamie j arnoldJamie J Arnold,david j filmanDavid J Filman,craig e cameronCraig E Cameron,james m hogleJames M Hogle,

    Poliovirus 3CD is a multifunctional protein that serves as a precursor to the protease 3C(pro) and the viral polymerase 3D(pol) and also plays a role in the control of viral replication. Although 3CD is a fully functional protease, it lacks polymerase activity. We have solved the crystal structures of 3CD at a 3.4-A resolution and the G64S fidelity mutant of 3D(pol) at a 3.0-A resolution. In the 3CD structure, the 3C and 3D domains are joined by a poorly ordered polypeptide linker, possibly to facilitate its cleavage, in an arrangement that precludes intramolecular proteolysis. The polymerase active site is intact in both the 3CD and the 3D(pol) G64S structures, despite the disruption of a network proposed to position key residues in the active site. Therefore, changes in molecular flexibility may be responsible for the differences in fidelity and polymerase activities. Extensive packing contacts between symmetry-related 3CD molecules and the approach of the 3C domain's N terminus to the VPg binding site suggest how 3D(pol) makes biologically relevant interactions with the 3C, 3CD, and 3BCD proteins that control the uridylylation of VPg during the initiation of viral replication. Indeed, mutations designed to disrupt these interfaces have pronounced effects on the uridylylation reaction in vitro.

    Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNA-dependent RNA polymerase. Publishing Authors By Initials

    ll marcotteLL Marcotte,ab wassAB Wass,dw goharaDW Gohara,hb pathakHB Pathak,jj arnoldJJ Arnold,dj filmanDJ Filman,ce cameronCE Cameron,jm hogleJM Hogle,

    For similar proteins: viral proteins research abstracts see: proteins: viral proteins research

    PUBMED ID PMID:

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    Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNA-dependent RNA polymerase. Journal Published:

    PUBLICATION TYPE: Research Support, N.I.H., Extr

    Journal: Journal of virology

    VOLUME: 81

    Page Numbers: 3583-96

    Journal Abbreviation: J. Virol.

    ISSN: 0022-538X

    DAY: 24

    MONTH: 01

    YEAR: 2007

    Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNA-dependent RNA polymerase. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 113724

    Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNA-dependent RNA polymerase. Keywords Mesh Terms:

    KEYWORDS: Viral Proteins

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNA-dependent RNA polymerase. Information

    Substance Name: 3C proteases

    Registry Number: EC 3.4.22.28

    Grant and Affiliation Information for Crystal structure of poliovirus 3CD protein: virally encoded protease and precursor to the RNA-dependent RNA polymerase.

    AFFILIATION: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIAID

    GRANT: R01 AI053531-05

    ACRONYM: AI

    MEDLINETA: J Virol

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

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