Structural Insight into the Stabilizing Effect of O‑Glycosylation
Protein glycosylation has been shown to have a variety of site-specific and glycan-specific effects, but so far, the molecular logic that leads to such observations has been elusive. Understanding the structural changes that occur and being able to correlate those with the physical properties of the...
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| Veröffentlicht in: | Biochemistry (Easton) 2017-06, Vol.56 (23), p.2897-2906 |
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| container_title | Biochemistry (Easton) |
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| creator | Chaffey, Patrick K Guan, Xiaoyang Chen, Chao Ruan, Yuan Wang, Xinfeng Tran, Amy H Koelsch, Theo N Cui, Qiu Feng, Yingang Tan, Zhongping |
| description | Protein glycosylation has been shown to have a variety of site-specific and glycan-specific effects, but so far, the molecular logic that leads to such observations has been elusive. Understanding the structural changes that occur and being able to correlate those with the physical properties of the glycopeptide are valuable steps toward being able to predict how specific glycosylation patterns will affect the stability of glycoproteins. By systematically comparing the structural features of the O-glycosylated carbohydrate-binding module of a Trichoderma reesei-derived Family 7 cellobiohydrolase, we were able to develop a better understanding of the influence of O-glycan structure on the molecule’s physical stability. Our results indicate that the previously observed stabilizing effects of O-glycans come from the introduction of new bonding interactions to the structure and increased rigidity, while the decreased stability seemed to result from the impaired interactions and increased conformational flexibility. This type of knowledge provides a powerful and potentially general mechanism for improving the stability of proteins through glycoengineering. |
| doi_str_mv | 10.1021/acs.biochem.7b00195 |
| format | Article |
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Understanding the structural changes that occur and being able to correlate those with the physical properties of the glycopeptide are valuable steps toward being able to predict how specific glycosylation patterns will affect the stability of glycoproteins. By systematically comparing the structural features of the O-glycosylated carbohydrate-binding module of a Trichoderma reesei-derived Family 7 cellobiohydrolase, we were able to develop a better understanding of the influence of O-glycan structure on the molecule’s physical stability. Our results indicate that the previously observed stabilizing effects of O-glycans come from the introduction of new bonding interactions to the structure and increased rigidity, while the decreased stability seemed to result from the impaired interactions and increased conformational flexibility. 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Understanding the structural changes that occur and being able to correlate those with the physical properties of the glycopeptide are valuable steps toward being able to predict how specific glycosylation patterns will affect the stability of glycoproteins. By systematically comparing the structural features of the O-glycosylated carbohydrate-binding module of a Trichoderma reesei-derived Family 7 cellobiohydrolase, we were able to develop a better understanding of the influence of O-glycan structure on the molecule’s physical stability. Our results indicate that the previously observed stabilizing effects of O-glycans come from the introduction of new bonding interactions to the structure and increased rigidity, while the decreased stability seemed to result from the impaired interactions and increased conformational flexibility. This type of knowledge provides a powerful and potentially general mechanism for improving the stability of proteins through glycoengineering.</description><subject>Amino Acid Substitution</subject><subject>Binding Sites</subject><subject>Cellulose 1,4-beta-Cellobiosidase - chemistry</subject><subject>Cellulose 1,4-beta-Cellobiosidase - metabolism</subject><subject>Enzyme Stability</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - metabolism</subject><subject>Glycoproteins - chemistry</subject><subject>Glycoproteins - metabolism</subject><subject>Glycoside Hydrolases - chemistry</subject><subject>Glycoside Hydrolases - metabolism</subject><subject>Glycosylation</subject><subject>Models, Molecular</subject><subject>Mutation</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Protein Processing, Post-Translational</subject><subject>Protein Unfolding</subject><subject>Trichoderma - enzymology</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kL1OwzAURi0EoqXwBEgoI0ta_zbxiKpSKlXqUJgtx3FaV0lcbGcoE6_AK_IkuGpgxMuVpfN9V_cAcI_gGEGMJlL5cWGs2ulmnBUQIs4uwBAxDFPKObsEQwjhNMV8Cgfgxvt9_FKY0WswwDnlFNFsCGab4DoVOifrZNl6s92FxLTBJmGnk02QhanNh2m3ybyqtAqJrZL19-fXoj4q64-1DMa2t-CqkrXXd_0cgbfn-evsJV2tF8vZ0yqVhLKQKlLiTOY64yUkqECxMC9LonFVIE0ILjhjumJYlbSEjJOMaMZUfFMJuaaajMDjuffg7HunfRCN8UrXtWy17bxAOecIZRCyiJIzqpz13ulKHJxppDsKBMXJnoj2RG9P9PZi6qFf0BWNLv8yv7oiMDkDp_Tedq6N9_5b-QNWoH-o</recordid><startdate>20170613</startdate><enddate>20170613</enddate><creator>Chaffey, Patrick K</creator><creator>Guan, Xiaoyang</creator><creator>Chen, Chao</creator><creator>Ruan, Yuan</creator><creator>Wang, Xinfeng</creator><creator>Tran, Amy H</creator><creator>Koelsch, Theo N</creator><creator>Cui, Qiu</creator><creator>Feng, Yingang</creator><creator>Tan, Zhongping</creator><general>American Chemical Society</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-9302-150X</orcidid></search><sort><creationdate>20170613</creationdate><title>Structural Insight into the Stabilizing Effect of O‑Glycosylation</title><author>Chaffey, Patrick K ; 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Understanding the structural changes that occur and being able to correlate those with the physical properties of the glycopeptide are valuable steps toward being able to predict how specific glycosylation patterns will affect the stability of glycoproteins. By systematically comparing the structural features of the O-glycosylated carbohydrate-binding module of a Trichoderma reesei-derived Family 7 cellobiohydrolase, we were able to develop a better understanding of the influence of O-glycan structure on the molecule’s physical stability. Our results indicate that the previously observed stabilizing effects of O-glycans come from the introduction of new bonding interactions to the structure and increased rigidity, while the decreased stability seemed to result from the impaired interactions and increased conformational flexibility. 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| subjects | Amino Acid Substitution Binding Sites Cellulose 1,4-beta-Cellobiosidase - chemistry Cellulose 1,4-beta-Cellobiosidase - metabolism Enzyme Stability Fungal Proteins - chemistry Fungal Proteins - metabolism Glycoproteins - chemistry Glycoproteins - metabolism Glycoside Hydrolases - chemistry Glycoside Hydrolases - metabolism Glycosylation Models, Molecular Mutation Nuclear Magnetic Resonance, Biomolecular Protein Conformation Protein Folding Protein Processing, Post-Translational Protein Unfolding Trichoderma - enzymology |
| title | Structural Insight into the Stabilizing Effect of O‑Glycosylation |
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