Naslov
Conformational study of Bacteroides thetaiotaomicron dipeptidyl peptidase III

Autori
Tomin, Marko ; Tomić, Sanja ; Sabljić, Igor

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

Izvornik
29th European Crystallographic Meeting, Book of Abstracts, Acta Crystallographica A, 71 / - , 2015, 209-209

Skup
29th European Crystallographic Meeting

Mjesto i datum
Rovinj, Hrvatska, 23.08.2015. - 28.08.2015

Vrsta sudjelovanja
Poster

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
dipeptidyl peptidase III ; computational

Sažetak
Dipeptidyl peptidase III isolated from Bacteroides thetaiotaomicron, Bt-DPP3, is a two-domain zinc exopeptidase from M49 family. Members of this family, characterized by their HEXXGH motive, cleave dipeptidyl residues from the N-terminus of their substrates. The crystallographically determined Bt-DPP3 structure, consisting of two domains separated by a wide cleft, strongly resembles 3D structure of the ortholog despite their low sequence identity (~23%). Our earlier computational study clearly showed that human DPP3 experiences long-range conformational changes in solution. We showed that, among a number of different forms that it can adopt, the compact form is the most stable and enzymatically active. In this work we used classical and accelerated MD to examine the conformational landscape of Bt-DPP3 as well as influence of ligand binding on the protein structure and dynamics. Special emphasis has been placed on the zinc ion coordination flexibility, since the existing data for human DPP3 suggests the high plasticity of the Zn2+ coordination.

Izvorni jezik
Engleski

Znanstvena područja
Kemija

POVEZANOST RADA