دورية أكاديمية
أعرض في EDS

Conformational flexibility of EptA driven by an interdomain helix provides insights for enzyme-substrate recognition.

التفاصيل البيبلوغرافية
العنوان: Conformational flexibility of EptA driven by an interdomain helix provides insights for enzyme-substrate recognition.
المؤلفون: Anandan A; School of Molecular Sciences, The University of Western Australia, 35 Stirling Highway, Perth 6009, Australia., Dunstan NW; School of Molecular Sciences, The University of Western Australia, 35 Stirling Highway, Perth 6009, Australia., Ryan TM; Australian Synchrotron, 800 Blackburn Road, Clayton, Victoria 3168, Australia., Mertens HDT; European Molecular Biology Laboratory, Hamburg Unit, DESY, Notkestrasse 85, 22607 Hamburg, Germany., Lim KYL; The Marshall Centre for Infectious Diseases Research and Training, School of Biomedical Sciences, University of Western Australia, 35 Stirling Highway, Perth, Western Australia 6009, Australia., Evans GL; School of Molecular Sciences, The University of Western Australia, 35 Stirling Highway, Perth 6009, Australia., Kahler CM; The Marshall Centre for Infectious Diseases Research and Training, School of Biomedical Sciences, University of Western Australia, 35 Stirling Highway, Perth, Western Australia 6009, Australia., Vrielink A; School of Molecular Sciences, The University of Western Australia, 35 Stirling Highway, Perth 6009, Australia.
المصدر: IUCrJ [IUCrJ] 2021 Jul 15; Vol. 8 (Pt 5), pp. 732-746. Date of Electronic Publication: 2021 Jul 15 (Print Publication: 2021).
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: International Union of Crystallography Country of Publication: England NLM ID: 101623101 Publication Model: eCollection Cited Medium: Print ISSN: 2052-2525 (Print) Linking ISSN: 20522525 NLM ISO Abbreviation: IUCrJ Subsets: PubMed not MEDLINE
أسماء مطبوعة: Original Publication: Chester : International Union of Crystallography, [2014]-
مستخلص: Many pathogenic gram-negative bacteria have developed mechanisms to increase resistance to cationic antimicrobial peptides by modifying the lipid A moiety. One modification is the addition of phospho-ethano-lamine to lipid A by the enzyme phospho-ethano-lamine transferase (EptA). Previously we reported the structure of EptA from Neisseria , revealing a two-domain architecture consisting of a periplasmic facing soluble domain and a transmembrane domain, linked together by a bridging helix. Here, the conformational flexibility of EptA in different detergent environments is probed by solution scattering and intrinsic fluorescence-quenching studies. The solution scattering studies reveal the enzyme in a more compact state with the two domains positioned close together in an n -do-decyl-β-d-maltoside micelle environment and an open extended structure in an n -do-decyl-phospho-choline micelle environment. Intrinsic fluorescence quenching studies localize the domain movements to the bridging helix. These results provide important insights into substrate binding and the molecular mechanism of endotoxin modification by EptA.
(© Anandhi Anandan et al. 2021.)
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فهرسة مساهمة: Keywords: EptA; conformational flexibility; enzyme substrate recognition; phosphoethanolamine transferase; small-angle X-ray scattering; tryptophan fluorescence
تواريخ الأحداث: Date Created: 20210929 Latest Revision: 20231107
رمز التحديث: 20240628
مُعرف محوري في PubMed: PMC8420757
DOI: 10.1107/S2052252521005613
PMID: 34584735
قاعدة البيانات: MEDLINE
الوصف
تدمد:2052-2525
DOI:10.1107/S2052252521005613