دورية أكاديمية
أعرض في EDS

Structure of MlaFB uncovers novel mechanisms of ABC transporter regulation.

التفاصيل البيبلوغرافية
العنوان: Structure of MlaFB uncovers novel mechanisms of ABC transporter regulation.
المؤلفون: Kolich LR; Department of Cell Biology, New York University School of Medicine, New York, United States., Chang YT; Department of Cell Biology, New York University School of Medicine, New York, United States., Coudray N; Department of Cell Biology, New York University School of Medicine, New York, United States.; Applied Bioinformatics Laboratory, New York University School of Medicine, New York, United States., Giacometti SI; Department of Cell Biology, New York University School of Medicine, New York, United States., MacRae MR; Department of Cell Biology, New York University School of Medicine, New York, United States., Isom GL; Department of Cell Biology, New York University School of Medicine, New York, United States., Teran EM; Department of Cell Biology, New York University School of Medicine, New York, United States., Bhabha G; Department of Cell Biology, New York University School of Medicine, New York, United States., Ekiert DC; Department of Cell Biology, New York University School of Medicine, New York, United States.; Department of Microbiology, New York University School of Medicine, New York, United States.
المصدر: ELife [Elife] 2020 Jun 30; Vol. 9. Date of Electronic Publication: 2020 Jun 30.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: eLife Sciences Publications, Ltd Country of Publication: England NLM ID: 101579614 Publication Model: Electronic Cited Medium: Internet ISSN: 2050-084X (Electronic) Linking ISSN: 2050084X NLM ISO Abbreviation: Elife Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Cambridge, UK : eLife Sciences Publications, Ltd., 2012-
مواضيع طبية MeSH: ATP-Binding Cassette Transporters/*metabolism , Escherichia coli Proteins/*metabolism, ATP-Binding Cassette Transporters/chemistry ; ATP-Binding Cassette Transporters/isolation & purification ; Escherichia coli/metabolism ; Escherichia coli Proteins/chemistry ; Escherichia coli Proteins/isolation & purification ; Molecular Structure
مستخلص: ABC transporters facilitate the movement of diverse molecules across cellular membranes, but how their activity is regulated post-translationally is not well understood. Here we report the crystal structure of MlaFB from E. coli , the cytoplasmic portion of the larger MlaFEDB ABC transporter complex, which drives phospholipid trafficking across the bacterial envelope to maintain outer membrane integrity. MlaB, a STAS domain protein, binds the ABC nucleotide binding domain, MlaF, and is required for its stability. Our structure also implicates a unique C-terminal tail of MlaF in self-dimerization. Both the C-terminal tail of MlaF and the interaction with MlaB are required for the proper assembly of the MlaFEDB complex and its function in cells. This work leads to a new model for how an important bacterial lipid transporter may be regulated by small proteins, and raises the possibility that similar regulatory mechanisms may exist more broadly across the ABC transporter family.
Competing Interests: LK, YC, NC, SG, MM, GI, ET, GB, DE No competing interests declared
(© 2020, Kolich et al.)
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معلومات مُعتمدة: T32 GM088118 United States NH NIH HHS; P30 GM124169 United States GM NIGMS NIH HHS; R35 GM128777 United States GM NIGMS NIH HHS; R00 GM112982 United States GM NIGMS NIH HHS; DFS-20-16 United States DRCRF Damon Runyon Cancer Research Foundation; T32 GM088118 United States GM NIGMS NIH HHS; R01 GM124149 United States GM NIGMS NIH HHS
فهرسة مساهمة: Keywords: ABC transporters; E. coli; MlaB; MlaF; STAS domain; bacterial outer membrane; molecular biophysics; structural biology; x-ray crystallography
سلسلة جزيئية: PDB 10.2210/pdb2mwg/pdb
المشرفين على المادة: 0 (ATP-Binding Cassette Transporters)
0 (Escherichia coli Proteins)
0 (MlaF protein, E coli)
تواريخ الأحداث: Date Created: 20200701 Date Completed: 20210226 Latest Revision: 20240427
رمز التحديث: 20240427
مُعرف محوري في PubMed: PMC7367683
DOI: 10.7554/eLife.60030
PMID: 32602838
قاعدة البيانات: MEDLINE
الوصف
تدمد:2050-084X
DOI:10.7554/eLife.60030