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The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding.

التفاصيل البيبلوغرافية
العنوان: The role of membrane destabilisation and protein dynamics in BAM catalysed OMP folding.
المؤلفون: White P; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.; GlaxoSmithKline R&D, Stevenage, UK., Haysom SF; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK., Iadanza MG; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.; Scientific Computing Department, Science and Technology Facilities Council, Didcot, UK., Higgins AJ; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK., Machin JM; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK., Whitehouse JM; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK., Horne JE; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK.; Department of Biochemistry, University of Oxford, Oxford, UK., Schiffrin B; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK., Carpenter-Platt C; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK., Calabrese AN; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK., Storek KM; Department of Infectious Diseases, Genentech Inc., South San Francisco, CA, USA., Rutherford ST; Department of Infectious Diseases, Genentech Inc., South San Francisco, CA, USA., Brockwell DJ; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK., Ranson NA; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK. n.a.ranson@leeds.ac.uk., Radford SE; Astbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, UK. s.e.radford@leeds.ac.uk.
المصدر: Nature communications [Nat Commun] 2021 Jul 07; Vol. 12 (1), pp. 4174. Date of Electronic Publication: 2021 Jul 07.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE
أسماء مطبوعة: Original Publication: [London] : Nature Pub. Group
مواضيع طبية MeSH: Protein Folding*, Bacterial Outer Membrane Proteins/*metabolism , Escherichia coli Proteins/*metabolism , Hydrolases/*metabolism , Liposomes/*metabolism, Bacterial Outer Membrane Proteins/genetics ; Bacterial Outer Membrane Proteins/isolation & purification ; Bacterial Outer Membrane Proteins/ultrastructure ; Cryoelectron Microscopy ; Dynamic Light Scattering ; Escherichia coli Proteins/genetics ; Escherichia coli Proteins/isolation & purification ; Escherichia coli Proteins/ultrastructure ; Hydrolases/genetics ; Hydrolases/isolation & purification ; Hydrolases/ultrastructure ; Lipid Metabolism ; Liposomes/ultrastructure ; Molecular Dynamics Simulation ; Protein Conformation, beta-Strand ; Proteolipids/metabolism ; Proteolipids/ultrastructure ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Recombinant Proteins/ultrastructure
مستخلص: The folding of β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria is catalysed by the β-barrel assembly machinery (BAM). How lateral opening in the β-barrel of the major subunit BamA assists in OMP folding, and the contribution of membrane disruption to BAM catalysis remain unresolved. Here, we use an anti-BamA monoclonal antibody fragment (Fab1) and two disulphide-crosslinked BAM variants (lid-locked (LL), and POTRA-5-locked (P5L)) to dissect these roles. Despite being lethal in vivo, we show that all complexes catalyse folding in vitro, albeit less efficiently than wild-type BAM. CryoEM reveals that while Fab1 and BAM-P5L trap an open-barrel state, BAM-LL contains a mixture of closed and contorted, partially-open structures. Finally, all three complexes globally destabilise the lipid bilayer, while BamA does not, revealing that the BAM lipoproteins are required for this function. Together the results provide insights into the role of BAM structure and lipid dynamics in OMP folding.
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معلومات مُعتمدة: BB/M012573/1 United Kingdom BB_ Biotechnology and Biological Sciences Research Council; MR/P01849/1 United Kingdom MRC_ Medical Research Council; BB/N007603/1 United Kingdom BB_ Biotechnology and Biological Sciences Research Council; MR/P018491/1 United Kingdom MRC_ Medical Research Council; BB/T000635/1 United Kingdom BB_ Biotechnology and Biological Sciences Research Council; 222373/Z/21/Z United Kingdom WT_ Wellcome Trust; 108466/Z/15/Z United Kingdom WT_ Wellcome Trust; United Kingdom WT_ Wellcome Trust; BB/M011151/1 United Kingdom BB_ Biotechnology and Biological Sciences Research Council; 105220/Z/14?Z United Kingdom WT_ Wellcome Trust
المشرفين على المادة: 0 (Bacterial Outer Membrane Proteins)
0 (BamA protein, E coli)
0 (Escherichia coli Proteins)
0 (Liposomes)
0 (Proteolipids)
0 (Recombinant Proteins)
0 (proteoliposomes)
134632-13-6 (OmpX protein, E coli)
149024-69-1 (OMPA outer membrane proteins)
EC 3.- (Hydrolases)
تواريخ الأحداث: Date Created: 20210708 Date Completed: 20210721 Latest Revision: 20230204
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC8263589
DOI: 10.1038/s41467-021-24432-x
PMID: 34234105
قاعدة البيانات: MEDLINE
الوصف
تدمد:2041-1723
DOI:10.1038/s41467-021-24432-x