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Conformational study of Bacteroides thetaiotaomicron dipeptidyl peptidase III (CROSBI ID 631544)

Prilog sa skupa u časopisu | sažetak izlaganja sa skupa | međunarodna recenzija

Tomin, Marko ; Tomić, Sanja ; Sabljić, Igor Conformational study of Bacteroides thetaiotaomicron dipeptidyl peptidase III // Acta crystallographica. Section A, Foundations and advances. 2015. str. 209-209 doi: 10.1107/S2053273315096850

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

Povezanost rada

Kemija

Poveznice
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