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Structural and dynamic evolution of the amphipathic N-terminus diversifies enzyme thermostability in the glycoside hydrolase family 12
Jiang, Xukai1; Chen, Guanjun1; Wang, Lushan1,2
2016-08-31
Source PublicationPHYSICAL CHEMISTRY CHEMICAL PHYSICS
ISSN1463-9076
Volume18Issue:31Pages:21340-21350
Abstract

Understanding the molecular mechanism underlying protein thermostability is central to the process of efficiently engineering thermostable cellulases, which can provide potential advantages in accelerating the conversion of biomass into clean biofuels. Here, we explored the general factors that diversify enzyme thermostability in the glycoside hydrolase family 12 (GH12) using comparative molecular dynamics (MD) simulations coupled to a bioinformatics approach. The results indicated that protein stability is not equally distributed over the whole structure: the N-terminus is the most thermal-sensitive region of the enzymes with a beta-sandwich architecture and it tends to lose its secondary structure during the course of protein unfolding. Furthermore, we found that the total interaction energy within the N-terminus is appreciably correlated with enzyme thermostability. Interestingly, the internal interactions within the N-terminus are organized in a special amphipathic pattern in which a hydrophobic packing cluster and a hydrogen bonding cluster lie at the two ends of the N-terminus. Finally, bioinformatics analysis demonstrated that the amphipathic pattern is highly conserved in GH12 and besides that, the evolution of the amino acids in the N-terminal region is an inherent mechanism underlying the diversity of enzyme thermostability. Taken together, our results demonstrate that the N-terminus is generally the structure that determines enzyme thermostability in GH12, and thereby it is also an ideal engineering target. The dynameomics study of a protein family can give a general view of protein functions, which will offer a wide range of applications in future protein engineering.

SubtypeArticle
WOS HeadingsScience & Technology ; Physical Sciences
DOI10.1039/c6cp02998a
Indexed BySCI
Language英语
WOS KeywordCOMPARATIVE MOLECULAR-DYNAMICS ; SITE ARCHITECTURE ANALYSIS ; THERMAL-STABILITY ; TRICHODERMA-REESEI ; PROTEIN STABILITY ; ELEVATED-TEMPERATURES ; BINDING SPECIFICITY ; UNFOLDING PATHWAY ; GH11 XYLANASE ; GROMACS 4.5
WOS Research AreaChemistry ; Physics
WOS SubjectChemistry, Physical ; Physics, Atomic, Molecular & Chemical
Funding OrganizationNational Natural Science Foundation of China(31370111/31170071) ; Key Technologies R&D Program of Shandong Province(2015GSF121019)
WOS IDWOS:000381418000044
Citation statistics
Document Type期刊论文
Identifierhttp://ir.ipe.ac.cn/handle/122111/21454
Collection多相复杂系统国家重点实验室
Affiliation1.Shandong Univ, State Key Lab Microbial Technol, Jinan 250100, Peoples R China
2.Chinese Acad Sci, Inst Proc Engn, State Key Lab Biochem Engn, Beijing 10090, Peoples R China
Recommended Citation
GB/T 7714
Jiang, Xukai,Chen, Guanjun,Wang, Lushan. Structural and dynamic evolution of the amphipathic N-terminus diversifies enzyme thermostability in the glycoside hydrolase family 12[J]. PHYSICAL CHEMISTRY CHEMICAL PHYSICS,2016,18(31):21340-21350.
APA Jiang, Xukai,Chen, Guanjun,&Wang, Lushan.(2016).Structural and dynamic evolution of the amphipathic N-terminus diversifies enzyme thermostability in the glycoside hydrolase family 12.PHYSICAL CHEMISTRY CHEMICAL PHYSICS,18(31),21340-21350.
MLA Jiang, Xukai,et al."Structural and dynamic evolution of the amphipathic N-terminus diversifies enzyme thermostability in the glycoside hydrolase family 12".PHYSICAL CHEMISTRY CHEMICAL PHYSICS 18.31(2016):21340-21350.
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