A linker of the proline-threonine repeating motif sequence is bimodal

Author(s)

Skaf, Munir Salomao ^[1] ; Polikarpov, Igor ^[2] ; Stankovic, Ivana M. ^{[1, 3]}

Affiliation

^[1] Univ Campinas UNICAMP, Inst Chem, POB 6154, BR-13082086 Campinas, SP - Brazil

^[2] Univ Sao Paulo, Sao Carlos Inst Phys, Ave Trabalhador Sao Carlense 400, BR-13560970 Sao Carlos, SP - Brazil

^[3] Univ Belgrade, Inst Chem Technol & Met, Njegoseva 12, Belgrade 11000 - Serbia

• Document type: Journal article
• Source: Journal of Molecular Modeling; v. 26, n. 7 JUN 19 2020.
• Web of Science Citations: 0

Abstract

The linker of the endoglucanase fromXanthomonas campestris pv. campestris((PT)(12)) has a specific sequence, a repeating proline-threonine motif. In order to understand its role, it has been compared to a regular sequence linker, in this work-the cellobiohydrolase 2 fromTrichoderma reesei(CBH2). Elastic properties of the two linkers have been estimated by calculating free energy profile along the linker length from an enhanced sampling molecular dynamics simulation. The (PT)(12)exhibits more pronounced elastic behaviour than CBH2. The PT repeating motif results in a two-mode energy profile which could be very useful in the enzyme motions along the substrate during hydrolytic catalysis. (AU)

• FAPESP's process: 08/56255-9 - Structure and function of enzymes and auxiliary proteins from Trichoderma, active in cell-wall hydrolysis
• Grantee: Igor Polikarpov
• Support Opportunities: Program for Research on Bioenergy (BIOEN) - Thematic Grants
• FAPESP's process: 10/08680-2 - Molecular aspectos of lignocellulosic biomass degradation: dynamics of enzymes and plant cell wall nanoarchitecture
• Grantee: Rodrigo Leandro Silveira
• Support Opportunities: Scholarships in Brazil - Doctorate
• FAPESP's process: 09/54035-4 - Facility for advanced studies of biosystems and nanostructured materials
• Grantee: Igor Polikarpov
• Support Opportunities: Multi-user Equipment Program