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Atomic resolution crystal structure of Sapp2p, a secreted aspartic protease from Candida parapsilosis

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F15%3A00454168" target="_blank" >RIV/61388963:_____/15:00454168 - isvavai.cz</a>

  • Alternative codes found

    RIV/68378050:_____/15:00454168

  • Result on the web

    <a href="http://dx.doi.org/10.1107/S1399004715019392" target="_blank" >http://dx.doi.org/10.1107/S1399004715019392</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1107/S1399004715019392" target="_blank" >10.1107/S1399004715019392</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Atomic resolution crystal structure of Sapp2p, a secreted aspartic protease from Candida parapsilosis

  • Original language description

    The virulence of the Candida pathogens is enhanced by the production of secreted aspartic proteases, which therefore represent possible targets for drug design. Here, the crystal structure of the secreted aspartic protease Sapp2p from Candida parapsilosis was determined. Sapp2p was isolated from its natural source and crystallized in complex with pepstatin A, a classical aspartic protease inhibitor. The atomic resolution of 0.83 angstrom allowed the protonation states of the active-site residues to be inferred. A detailed comparison of the structure of Sapp2p with the structure of Sapp1p, the most abundant C. parapsilosis secreted aspartic protease, was performed. The analysis, which included advanced quantum-chemical interaction-energy calculations, uncovered molecular details that allowed the experimentally observed equipotent inhibition of both isoenzymes by pepstatin A to be rationalized.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

  • CEP classification

    CE - Biochemistry

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/GA14-23022S" target="_blank" >GA14-23022S: Structural studies of aspartic protease from Candida parapsilosis as a tool for design of antimycotic compounds.</a><br>

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2015

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Acta Crystallographica Section D-Biological Crystalloghraphy

  • ISSN

    1399-0047

  • e-ISSN

  • Volume of the periodical

    71

  • Issue of the periodical within the volume

    12

  • Country of publishing house

    DK - DENMARK

  • Number of pages

    11

  • Pages from-to

    2494-2504

  • UT code for WoS article

    000365773900012

  • EID of the result in the Scopus database

    2-s2.0-84948798309