دورية أكاديمية
أعرض في EDS

Conservation of knotted and slipknotted topology in transmembrane transporters.

التفاصيل البيبلوغرافية
العنوان: Conservation of knotted and slipknotted topology in transmembrane transporters.
المؤلفون: Zayats V; Centre of New Technologies, University of Warsaw, Warsaw, Poland., Sikora M; Centre of New Technologies, University of Warsaw, Warsaw, Poland; Faculty of Mathematics, Informatics and Mechanics, University of Warsaw, Warsaw, Poland., Perlinska AP; Centre of New Technologies, University of Warsaw, Warsaw, Poland., Stasiulewicz A; Centre of New Technologies, University of Warsaw, Warsaw, Poland; Department of Drug Chemistry, Faculty of Pharmacy, Medical University of Warsaw, Warsaw, Poland., Gren BA; Centre of New Technologies, University of Warsaw, Warsaw, Poland., Sulkowska JI; Centre of New Technologies, University of Warsaw, Warsaw, Poland. Electronic address: jsulkowska@cent.uw.edu.pl.
المصدر: Biophysical journal [Biophys J] 2023 Dec 05; Vol. 122 (23), pp. 4528-4541. Date of Electronic Publication: 2023 Nov 02.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Cell Press Country of Publication: United States NLM ID: 0370626 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1542-0086 (Electronic) Linking ISSN: 00063495 NLM ISO Abbreviation: Biophys J Subsets: MEDLINE
أسماء مطبوعة: Publication: Cambridge, MA : Cell Press
Original Publication: New York, Published by Rockefeller University Press [etc.] for the Biophysical Society.
مواضيع طبية MeSH: Protein Folding* , Membrane Transport Proteins*, Protein Conformation ; Membrane Proteins
مستخلص: The existence of nontrivial topology is well accepted in globular proteins but not in membrane proteins. Our comprehensive topological analysis of the Protein Data Bank structures reveals 18 families of transmembrane proteins with nontrivial topology, showing that they constitute a significant number of membrane proteins. Moreover, we found that they comprise one of the largest groups of secondary active transporters. We classified them based on their knotted fingerprint into four groups: three slipknotted and one knotted. Unexpectedly, we found that the same protein can possess two distinct slipknot motifs that correspond to its outward- and inward-open conformational state. Based on the analysis of structures and knotted fingerprints, we show that slipknot topology is directly involved in the conformational transition and substrate transfer. Therefore, entanglement can be used to classify proteins and to find their structure-function relationship. Furthermore, based on the topological analysis of the transmembrane protein structures predicted by AlphaFold, we identified new potentially slipknotted protein families.
Competing Interests: Declaration of interests The authors declare no competing interests.
(Copyright © 2023. Published by Elsevier Inc.)
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المشرفين على المادة: 0 (Membrane Transport Proteins)
0 (Membrane Proteins)
تواريخ الأحداث: Date Created: 20231103 Date Completed: 20231211 Latest Revision: 20240201
رمز التحديث: 20240201
مُعرف محوري في PubMed: PMC10719070
DOI: 10.1016/j.bpj.2023.10.031
PMID: 37919904
قاعدة البيانات: MEDLINE
الوصف
تدمد:1542-0086
DOI:10.1016/j.bpj.2023.10.031