Naslov
Protein-protein interactions between the adenylation and peptidyl carrier domain in tyrocidine sythetase 1

Autori
Šprung, Matilda ; Bučević-Popović, Viljemka ; Orhanović, Stjepan ; Soldo, Barbara ; Pavela-Vrančić, Maja

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

Izvornik
Supramolecular structure and function / Pifat-Mrzljak, Greta ; Zahradka, Ksenija - Zagreb : Institut Ruđer Bošković, 2009

ISBN
978-953-6690-81-7

Skup
Tenth international summer school on biophysics

Mjesto i datum
Rovinj, Hrvatska, 19.09.2009. - 01.10.2009

Vrsta sudjelovanja
Poster

Vrsta recenzije
Nije recenziran

Ključne riječi
Tyrocidine synthetase 1; conformational changes; protein-protein interactions

Sažetak
Tyrocidine synthetase 1 (TY1), produced by Bacillus brevis ATCC8185, is a non ribosomal peptide synthetase which consists of a single multifunctional polypeptide chain catalyzing the activation, thioesterification and epimerization of phenylalanine (Phe), the first amino acid to be incorporated into the tyrocidine antibiotic. The adenylation (A) domain is responsible for substrate uptake and its activation in form of an amino-acyl adenylate, which is then covalently attached in form of a thioester to the peptidyl-carrier protein (PCP) domain and subsequently epimerized by the epimerization (E) domain. During the catalytic course, domain A undergoes extensive conformational rearrangements, known as domain alternation. Two conformations have been proposed, the adenylate-forming conformation and the thioesterase-forming conformation responsible for the first and the second half reactions, respectively. Up to date, several crystal structures of the adenylate-forming enzymes in both conformations have been reported. The PCP domain was also shown to undergo various conformational changes that affect its recognition by specific partner proteins. Residues and regions at the surface of the PCP domain, responsible for protein-protein interactions have been identified. However, a protein recognition surface on the A domain, that could be critical for its interaction with the PCP domain, remains unidentified so far. Our present work is focused on investigating the A domain for putative protein-protein interaction surfaces by means of model building based on sequence homology and site-directed mutational studies.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

POVEZANOST RADA