دورية أكاديمية
YbtT is a low-specificity type II thioesterase that maintains production of the metallophore yersiniabactin in pathogenic enterobacteria.
العنوان: | YbtT is a low-specificity type II thioesterase that maintains production of the metallophore yersiniabactin in pathogenic enterobacteria. |
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المؤلفون: | Ohlemacher SI; From the Center for Women's Infectious Diseases Research.; Division of Infectious Diseases.; Department of Internal Medicine, and., Xu Y; From the Center for Women's Infectious Diseases Research.; Division of Infectious Diseases.; Department of Internal Medicine, and., Kober DL; Department of Internal Medicine, and.; Division of Pulmonary and Critical Care Medicine.; Department of Cell Biology and Physiology, Washington University, St. Louis, Missouri 63110 and., Malik M; From the Center for Women's Infectious Diseases Research.; Division of Infectious Diseases.; Department of Internal Medicine, and., Nix JC; the Molecular Biology Consortium, Advanced Light Source, Lawrence Berkeley National Laboratory, Berkeley, California 94720., Brett TJ; Department of Internal Medicine, and tbrett@wustl.edu.; Division of Pulmonary and Critical Care Medicine.; Department of Cell Biology and Physiology, Washington University, St. Louis, Missouri 63110 and., Henderson JP; From the Center for Women's Infectious Diseases Research, hendersonj@wustl.edu.; Division of Infectious Diseases.; Department of Internal Medicine, and. |
المصدر: | The Journal of biological chemistry [J Biol Chem] 2018 Dec 21; Vol. 293 (51), pp. 19572-19585. Date of Electronic Publication: 2018 Oct 24. |
نوع المنشور: | Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. |
اللغة: | English |
بيانات الدورية: | Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE |
أسماء مطبوعة: | Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology |
مواضيع طبية MeSH: | Enterobacteriaceae/*enzymology , Fatty Acid Synthases/*chemistry , Fatty Acid Synthases/*metabolism , Phenols/*metabolism , Thiazoles/*metabolism , Thiolester Hydrolases/*chemistry , Thiolester Hydrolases/*metabolism, Biocatalysis ; Catalytic Domain ; Crystallography, X-Ray ; Enterobacteriaceae/metabolism ; Fatty Acid Synthases/genetics ; Hydrolysis ; Kinetics ; Models, Molecular ; Mutation ; Thiolester Hydrolases/genetics |
مستخلص: | Clinical isolates of Yersinia , Klebsiella , and Escherichia coli frequently secrete the small molecule metallophore yersiniabactin (Ybt), which passivates and scavenges transition metals during human infections. YbtT is encoded within the Ybt biosynthetic operon and is critical for full Ybt production in bacteria. However, its biosynthetic function has been unclear because it is not essential for Ybt production by the in vitro reconstituted nonribosomal peptide synthetase/polyketide synthase (NRPS/PKS) pathway. Here, we report the structural and biochemical characterization of YbtT. YbtT structures at 1.4-1.9 Å resolution possess a serine hydrolase catalytic triad and an associated substrate chamber with features similar to those previously reported for low-specificity type II thioesterases (TEIIs). We found that YbtT interacts with the two major Ybt biosynthetic proteins, HMWP1 (high-molecular-weight protein 1) and HMWP2 (high-molecular-weight protein 2), and hydrolyzes a variety of aromatic and acyl groups from their phosphopantetheinylated carrier protein domains. In vivo YbtT titration in uropathogenic E. coli revealed a distinct optimum for Ybt production consistent with a tradeoff between clearing both stalled inhibitory intermediates and productive Ybt precursors from HMWP1 and HMWP2. These results are consistent with a model in which YbtT maintains cellular Ybt biosynthesis by removing nonproductive, inhibitory thioesters that form aberrantly at multiple sites on HMWP1 and HMWP2. Competing Interests: The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. |
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معلومات مُعتمدة: | R01 DK111930 United States DK NIDDK NIH HHS; T32 AI007172 United States AI NIAID NIH HHS; T32 GM007067 United States GM NIGMS NIH HHS; R01 DK099534 United States DK NIDDK NIH HHS; R01 HL119813 United States HL NHLBI NIH HHS |
فهرسة مساهمة: | Keywords: Escherichia coli (E. coli); biosynthesis; crystallography; editing thioesterase; mass spectrometry (MS); metal uptake; metallophore; siderophore; thioesterase; virulence; yersiniabactin |
سلسلة جزيئية: | PDB 6BA8; 6BA9; 3QMV; 3FLB; 4XJV; 3QMW |
المشرفين على المادة: | 0 (Phenols) 0 (Thiazoles) 0 (yersiniabactin) EC 2.3.1.85 (Fatty Acid Synthases) EC 3.1.2.- (Thiolester Hydrolases) EC 3.1.2.- (thioesterase II) |
تواريخ الأحداث: | Date Created: 20181026 Date Completed: 20190415 Latest Revision: 20240408 |
رمز التحديث: | 20240408 |
مُعرف محوري في PubMed: | PMC6314147 |
DOI: | 10.1074/jbc.RA118.005752 |
PMID: | 30355735 |
قاعدة البيانات: | MEDLINE |
تدمد: | 1083-351X |
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DOI: | 10.1074/jbc.RA118.005752 |