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

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/68378050:_____/15:00454168

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

—

Projekt

<a href="/cs/project/GA14-23022S" target="_blank" >GA14-23022S: Strukturní studie aspartátové proteázy z kvasinky Candida parapsilosis jako nástroj pro návrh antimykotik.</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Acta Crystallographica Section D-Biological Crystalloghraphy

ISSN

1399-0047

e-ISSN

—

Svazek periodika

71

Číslo periodika v rámci svazku

12

Stát vydavatele periodika

DK - Dánské království

Počet stran výsledku

11

Strana od-do

2494-2504

Kód UT WoS článku

000365773900012

EID výsledku v databázi Scopus

2-s2.0-84948798309