DC Field | Value | Language |
---|---|---|
dc.contributor.author | Hwang, Wonseok | ko |
dc.contributor.author | Yoo, Jungmin | ko |
dc.contributor.author | Lee, Yuno | ko |
dc.contributor.author | Park, Suyeon | ko |
dc.contributor.author | Phuong Lien Hoang | ko |
dc.contributor.author | Cho, HyeokJin | ko |
dc.contributor.author | Yu, Jeongmin | ko |
dc.contributor.author | Thi Minh Hoa Vo | ko |
dc.contributor.author | Shin, Minsang | ko |
dc.contributor.author | Jin, Mi Sun | ko |
dc.contributor.author | Park, Daeho | ko |
dc.contributor.author | Hyeon, Changbong | ko |
dc.contributor.author | Lee, Gwangrog | ko |
dc.date.accessioned | 2023-09-12T01:01:17Z | - |
dc.date.available | 2023-09-12T01:01:17Z | - |
dc.date.created | 2023-09-12 | - |
dc.date.issued | 2018-10 | - |
dc.identifier.citation | NATURE COMMUNICATIONS, v.9 | - |
dc.identifier.issn | 2041-1723 | - |
dc.identifier.uri | http://hdl.handle.net/10203/312440 | - |
dc.description.abstract | Metal ions at the active site of an enzyme act as cofactors, and their dynamic fluctuations can potentially influence enzyme activity. Here, we use lambda-exonuclease as a model enzyme with two Mg2+ binding sites and probe activity at various concentrations of magnesium by single-molecule-FRET. We find that while Mg-A(2+) and Mg-B(2+) have similar binding constants, the dissociation rate of Mg-A(2+) is two order of magnitude lower than that of Mg-B(2+) due to a kinetic-barrier-difference. At physiological Mg2+ concentration, the Mg-B(2+) ion near the 5'-terminal side of the scissile phosphate dissociates each-round of degradation, facilitating a series of DNA cleavages via fast product-release concomitant with enzyme-translocation. At a low magnesium concentration, occasional dissociation and slow re-coordination of Mg-A(2+) result in pauses during processive degradation. Our study highlights the importance of metal-ion-coordination dynamics in correlation with the enzymatic reaction-steps, and offers insights into the origin of dynamic heterogeneity in enzymatic catalysis. | - |
dc.language | English | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.title | Dynamic coordination of two-metal-ions orchestrates lambda-exonuclease catalysis | - |
dc.type | Article | - |
dc.identifier.wosid | 000448044300002 | - |
dc.identifier.scopusid | 2-s2.0-85055462830 | - |
dc.type.rims | ART | - |
dc.citation.volume | 9 | - |
dc.citation.publicationname | NATURE COMMUNICATIONS | - |
dc.identifier.doi | 10.1038/s41467-018-06750-9 | - |
dc.contributor.localauthor | Lee, Gwangrog | - |
dc.contributor.nonIdAuthor | Hwang, Wonseok | - |
dc.contributor.nonIdAuthor | Yoo, Jungmin | - |
dc.contributor.nonIdAuthor | Lee, Yuno | - |
dc.contributor.nonIdAuthor | Park, Suyeon | - |
dc.contributor.nonIdAuthor | Phuong Lien Hoang | - |
dc.contributor.nonIdAuthor | Cho, HyeokJin | - |
dc.contributor.nonIdAuthor | Yu, Jeongmin | - |
dc.contributor.nonIdAuthor | Thi Minh Hoa Vo | - |
dc.contributor.nonIdAuthor | Shin, Minsang | - |
dc.contributor.nonIdAuthor | Jin, Mi Sun | - |
dc.contributor.nonIdAuthor | Park, Daeho | - |
dc.contributor.nonIdAuthor | Hyeon, Changbong | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | METAL-IONS | - |
dc.subject.keywordPlus | RESTRICTION-ENDONUCLEASE | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURES | - |
dc.subject.keywordPlus | RIBONUCLEASE-H | - |
dc.subject.keywordPlus | DNA | - |
dc.subject.keywordPlus | HETEROGENEITY | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | PROCESSIVITY | - |
dc.subject.keywordPlus | SPECIFICITY | - |
dc.subject.keywordPlus | INHIBITION | - |
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