Ligand-Mediated Folding of the OmpA Periplasmic Domain from Acinetobacter baumannii
DC Field | Value | Language |
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dc.contributor.author | Mushtaq, Ameeq Ul | - |
dc.contributor.author | Park, Jeong Soon | - |
dc.contributor.author | Bae, Sung-Hun | - |
dc.contributor.author | Kim, Hye-Yeon | - |
dc.contributor.author | Yeo, Kwon Joo | - |
dc.contributor.author | Hwang, Eunha | - |
dc.contributor.author | Lee, Ki Yong | - |
dc.contributor.author | Jee, Jun-Goo | - |
dc.contributor.author | Cheong, Hae-Kap | - |
dc.contributor.author | Jeon, Young Ho | - |
dc.date.accessioned | 2021-09-03T06:03:04Z | - |
dc.date.available | 2021-09-03T06:03:04Z | - |
dc.date.created | 2021-06-16 | - |
dc.date.issued | 2017-05-23 | - |
dc.identifier.issn | 0006-3495 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/83432 | - |
dc.description.abstract | The periplasmic domain of OmpA from Acinetobacter baumannii (AbOmpA-PD) binds to diaminopimelate and anchors the outer membrane to the peptidoglycan layer in the cell wall. Although the crystal structure of AbOmpA-PD with its ligands has been reported, the mechanism of ligand-mediated folding of AbOmpA remains elusive. Here, we report that in vitro refolded apo-AbOmpA-PD in the absence of ligand exists as a mixture of two partially folded forms in solution: mostly unfolded (apo-state I) and hololike (apo-state II) states. Binding of the diaminopimelate or glycine ligand induced complete folding of AbOmpA-PD. The apo-state I was highly flexible and contained some secondary structural elements, whereas the apo-state II closely resembled the holo-state in terms of both structure and backbone dynamics, except for the ligand-binding region. N-15-relaxation-dispersion analyses for apo-state II revealed substantial motion on a millisecond timescale of residues in the H3 helix near the ligand-binding site, with this motion disappearing upon ligand binding. These results provide an insight into the ligand-mediated folding mechanism of AbOmpA-PD in solution. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | CELL PRESS | - |
dc.subject | MODEL-FREE APPROACH | - |
dc.subject | MAGNETIC-RESONANCE RELAXATION | - |
dc.subject | BACKBONE DYNAMICS | - |
dc.subject | OUTER-MEMBRANE | - |
dc.subject | PROTEIN | - |
dc.subject | MACROMOLECULES | - |
dc.subject | PEPTIDOGLYCAN | - |
dc.subject | SPECTROSCOPY | - |
dc.subject | MECHANISM | - |
dc.subject | STATES | - |
dc.title | Ligand-Mediated Folding of the OmpA Periplasmic Domain from Acinetobacter baumannii | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Lee, Ki Yong | - |
dc.contributor.affiliatedAuthor | Jeon, Young Ho | - |
dc.identifier.doi | 10.1016/j.bpj.2017.04.015 | - |
dc.identifier.scopusid | 2-s2.0-85019751309 | - |
dc.identifier.wosid | 000402119300009 | - |
dc.identifier.bibliographicCitation | BIOPHYSICAL JOURNAL, v.112, no.10, pp.2089 - 2098 | - |
dc.relation.isPartOf | BIOPHYSICAL JOURNAL | - |
dc.citation.title | BIOPHYSICAL JOURNAL | - |
dc.citation.volume | 112 | - |
dc.citation.number | 10 | - |
dc.citation.startPage | 2089 | - |
dc.citation.endPage | 2098 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.subject.keywordPlus | MODEL-FREE APPROACH | - |
dc.subject.keywordPlus | MAGNETIC-RESONANCE RELAXATION | - |
dc.subject.keywordPlus | BACKBONE DYNAMICS | - |
dc.subject.keywordPlus | OUTER-MEMBRANE | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | MACROMOLECULES | - |
dc.subject.keywordPlus | PEPTIDOGLYCAN | - |
dc.subject.keywordPlus | SPECTROSCOPY | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | STATES | - |
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