Naslov
Crystal structure of a mutant of the B subunit of heat-labile enterotoxin from E coli

Autori
Matković-Čalogović, Dubravka ; Loreggian, Arianna ; D˘Acunto, Maria ; Rosa ; Battistutta, Roberto ; Palu, Giorgio ; Zanotti, Giuseppe

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Book of Abstracts / Leban, Ivan ; Petrovčič, Nina - Ljubljana : Laboratory of Inorganic Chemistry, 1998, 51-51

Skup
7th Slovenian-Croatian Crystallographic Meeting

Mjesto i datum
Radenci, Slovenija, 18.06.1998. - 20.06.1998

Vrsta sudjelovanja
Predavanje

Vrsta recenzije
Nije recenziran

Ključne riječi
crystal structure; ribonucleotide reductase; anti-herpes simplex virus activity

Sažetak
Ribonucleotide reductase is a virally encoded enzyme from Herpes simplex virus (HSV), which consists of two subunits that form a tetrameric complex a2b2. The assembly of the protein is inhibited in vitro by nonapeptide, also termed R2, that corresponds to the carboxy terminal chain of the b subunit. In order to allow the correct delivery of this peptide into the infected cells, a fusion protein between the nonapeptide (YAGAVVNDL) and the B subunit of the heat-labile enterotoxin was constructed. This fusion product (EtB-R2) has been cloned and expressed in vibrio sp60 and th produced protein purified and crystallized. Crystals of EtB-R2 belong to space group P41212, with a = b = 127.23 A, c = 174.19 A. The structure solution has demonstrated the presence of one pentameric molecule per asymmetric unit, corresponding to a solvent content of about 75%.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

POVEZANOST RADA