Conformational study of Bacteroides thetaiotaomicron dipeptidyl peptidase III (CROSBI ID 631544)
Prilog sa skupa u časopisu | sažetak izlaganja sa skupa | međunarodna recenzija
Podaci o odgovornosti
Tomin, Marko ; Tomić, Sanja ; Sabljić, Igor
engleski
Conformational study of Bacteroides thetaiotaomicron dipeptidyl peptidase III
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.
dipeptidyl peptidase III ; computational
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Podaci o prilogu
209-209.
2015.
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objavljeno
10.1107/S2053273315096850
Podaci o matičnoj publikaciji
Acta crystallographica. Section A, Foundations and advances
2053-2733
Podaci o skupu
29th European Crystallographic meeting
poster
23.08.2015-28.08.2015
Rovinj, Hrvatska