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Ligand-Mediated Folding of the OmpA Periplasmic Domain from Acinetobacter baumannii

Authors
Mushtaq, Ameeq UlPark, Jeong SoonBae, Sung-HunKim, Hye-YeonYeo, Kwon JooHwang, EunhaLee, Ki YongJee, Jun-GooCheong, Hae-KapJeon, Young Ho
Issue Date
23-5월-2017
Publisher
CELL PRESS
Citation
BIOPHYSICAL JOURNAL, v.112, no.10, pp.2089 - 2098
Indexed
SCIE
SCOPUS
Journal Title
BIOPHYSICAL JOURNAL
Volume
112
Number
10
Start Page
2089
End Page
2098
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/83432
DOI
10.1016/j.bpj.2017.04.015
ISSN
0006-3495
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.
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약학대학 (약학과)
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