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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2023.6
- 수록면
- 21 - 27 (7page)
- DOI
- 10.34184/kssb.2023.11.2.21
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초록· 키워드
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The HlyBD-TolC complex, belonging to the type I secretion system (T1SS), is found in many pathogenic Gram-negative bacteria. This complex comprises three components: the ABC-type inner membrane transporter HlyB, the periplasmic adaptor HlyD, and the outer membrane channel TolC. Recent crystal and cryo-EM structures have shed light on the stoichiometry of the HlyB hexamer and HlyD hexamer in the functional complex. In this study, we performed a modeling study using the AI-based structure prediction program Alphafold-multimer to gain a deeper understanding of the assembly of the T1SS system. The program predicted a funnel-like hexameric model of the HlyD, which was stable in a molecular dynamics simulation, and the HlyD hexamer would intermesh with the TolC trimer in a cogwheel structure. Combining the modeled and docked structures, we built an assembly model of HlyBD-TolC, showing a central channel spanning the complex. These observations suggest a mechanism reminiscent of the DNA helicase.
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