Academic Journal
The oligomeric state of chitooligosaccharide deacetylase from the marine bacterium Vibrio campbellii.
| Τίτλος: | The oligomeric state of chitooligosaccharide deacetylase from the marine bacterium Vibrio campbellii. |
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| Συγγραφείς: | Pongnan S; School of Biomolecular Science and Engineering (BSE), Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong, Thailand., Robinson RC; School of Biomolecular Science and Engineering (BSE), Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong, Thailand., Kamonsutthipaijit N; Synchrotron Light Research Institute (Public Organization), Nakhon Ratchasima, Thailand., Fukamizo T; School of Biomolecular Science and Engineering (BSE), Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong, Thailand. Electronic address: tamo.f@vistec.ac.th., Suginta W; School of Biomolecular Science and Engineering (BSE), Vidyasirimedhi Institute of Science and Technology (VISTEC), Rayong, Thailand. Electronic address: wipa.s@vistec.ac.th. |
| Πηγή: | Biophysical reports [Biophys Rep (N Y)] 2026 Sep 09; Vol. 6 (3), pp. 100275. Date of Electronic Publication: 2026 Jun 24. |
| Τύπος έκδοσης: | Journal Article |
| Γλώσσα: | English |
| Στοιχεία περιοδικού: | Publisher: Cell Press Elsevier Country of Publication: United States NLM ID: 9918266001106676 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2667-0747 (Electronic) Linking ISSN: 26670747 NLM ISO Abbreviation: Biophys Rep (N Y) Subsets: MEDLINE |
| Imprint Name(s): | Original Publication: [New York] : Cell Press Elsevier, [2021]- |
| Ιατρικοί όροι (MeSH): | Vibrio*/enzymology , Amidohydrolases*/chemistry , Amidohydrolases*/metabolism , Bacterial Proteins*/chemistry , Protein Multimerization*, Models, Molecular |
| Περίληψη: | The crystal structure of a chitooligosaccharide deacetylase (COD) from the marine bacterium Vibrio campbellii (formerly V. harveyi), referred to as VhCOD, exhibits a homodimeric assembly, consistent with previously reported X-ray structures of related Vibrio CODs. Here, we investigated whether this dimeric assembly is retained in solution. Native polyacrylamide gel electrophoresis (native PAGE) analysis revealed that VhCOD is monomeric in solution, with dimeric species present only as a minor population. Small-angle X-ray scattering further indicated that VhCOD preferentially adopts a monomeric state under dilute solution conditions. Analysis of the published crystal structures using PISA/jsPISA (Protein Interfaces, Surfaces and Assemblies/JavaScript version) predicted relatively weak monomer-monomer interactions and suggested that homodimer formation occurs only at sufficiently high protein concentrations (>5 mg·mL-1). Chemical cross-linking experiments showed that macromolecular crowding reagents promote the formation of cross-linked dimer species. Taken together, we concluded that homodimerization of Vibrio CODs arises under crowded conditions rather than representing a dominant state. This interpretation is consistent with the physiological context of VhCOD as a secretory protein that is translocated through the crowded periplasm, where transient dimerization may be relevant prior to final export across the outer membrane. (Copyright © 2026 The Author(s). Published by Elsevier Inc. All rights reserved.) |
| Competing Interests: | Declaration of interests The authors declare no competing interests. |
| Contributed Indexing: | Keywords: PISA; SAXS; Vibrio campbellii; chitooligosaccharide deacetylase; homodimer |
| Substance Nomenclature: | EC 3.5.- (Amidohydrolases) 0 (Bacterial Proteins) EC 3.5.1.41 (chitin deacetylase) |
| SCR Organism: | Vibrio campbellii |
| Entry Date(s): | Date Created: 20260624 Date Completed: 20260909 Latest Revision: 20260909 |
| Update Code: | 20260910 |
| PubMed Central ID: | PMC13356635 |
| DOI: | 10.1016/j.bpr.2026.100275 |
| PMID: | 42341985 |
| Βάση Δεδομένων: | MEDLINE |
| ISSN: | 2667-0747 |
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| DOI: | 10.1016/j.bpr.2026.100275 |