دورية أكاديمية
Reciprocal allostery arising from a bienzyme assembly controls aromatic amino acid biosynthesis in Prevotella nigrescens.
| العنوان: | Reciprocal allostery arising from a bienzyme assembly controls aromatic amino acid biosynthesis in Prevotella nigrescens. |
|---|---|
| المؤلفون: | Bai Y; Maurice Wilkins Centre, Ferrier Research Institute, Victoria University of Wellington, Wellington, New Zealand., Parker EJ; Maurice Wilkins Centre, Ferrier Research Institute, Victoria University of Wellington, Wellington, New Zealand. Electronic address: emily.parker@vuw.ac.nz. |
| المصدر: | The Journal of biological chemistry [J Biol Chem] 2021 Sep; Vol. 297 (3), pp. 101038. Date of Electronic Publication: 2021 Jul 31. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| 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: | 3-Deoxy-7-Phosphoheptulonate Synthase/*chemistry , 3-Deoxy-7-Phosphoheptulonate Synthase/*metabolism , Amino Acids, Aromatic/*biosynthesis , Bacterial Proteins/*chemistry , Bacterial Proteins/*metabolism , Prevotella nigrescens/*metabolism, 3-Deoxy-7-Phosphoheptulonate Synthase/genetics ; Allosteric Regulation ; Amino Acid Sequence ; Bacterial Proteins/genetics ; Biosynthetic Pathways ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/metabolism ; Prevotella nigrescens/chemistry ; Prevotella nigrescens/enzymology ; Prevotella nigrescens/genetics ; Protein Domains ; Scattering, Small Angle ; Sequence Alignment |
| مستخلص: | Modular protein assembly has been widely reported as a mechanism for constructing allosteric machinery. Recently, a distinctive allosteric system has been identified in a bienzyme assembly comprising a 3-deoxy-d-arabino heptulosonate-7-phosphate synthase (DAH7PS) and chorismate mutase (CM). These enzymes catalyze the first and branch point reactions of aromatic amino acid biosynthesis in the bacterium Prevotella nigrescens (PniDAH7PS), respectively. The interactions between these two distinct catalytic domains support functional interreliance within this bifunctional enzyme. The binding of prephenate, the product of CM-catalyzed reaction, to the CM domain is associated with a striking rearrangement of overall protein conformation that alters the interdomain interactions and allosterically inhibits the DAH7PS activity. Here, we have further investigated the complex allosteric communication demonstrated by this bifunctional enzyme. We observed allosteric activation of CM activity in the presence of all DAH7PS substrates. Using small-angle X-ray scattering (SAXS) experiments, we show that changes in overall protein conformations and dynamics are associated with the presence of different DAH7PS substrates and the allosteric inhibitor prephenate. Furthermore, we have identified an extended interhelix loop located in CM domain, loop Competing Interests: Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article. (Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.) |
| فهرسة مساهمة: | Keywords: 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase; bifunctional enzyme; chorismate mutase; dynamic interactions; functional interdependency; interdomain interaction; reciprocal allostery; shikimate pathway |
| المشرفين على المادة: | 0 (Amino Acids, Aromatic) 0 (Bacterial Proteins) 0 (Enzyme Inhibitors) EC 2.5.1.54 (3-Deoxy-7-Phosphoheptulonate Synthase) |
| تواريخ الأحداث: | Date Created: 20210803 Date Completed: 20211208 Latest Revision: 20211214 |
| رمز التحديث: | 20221213 |
| مُعرف محوري في PubMed: | PMC8408635 |
| DOI: | 10.1016/j.jbc.2021.101038 |
| PMID: | 34343567 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1083-351X |
|---|---|
| DOI: | 10.1016/j.jbc.2021.101038 |