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Crystal structure of BtrK, a decarboxylase involved in the (S)-4-amino-2-hydroxybutyrate (AHBA) formation during butirosin biosynthesis
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Rivas Arenas, Laura A., de Paiva, Fernanda C. R., de O. Rossini, Nicolas, Li, YanYan, Spencer, Jonathan, Leadlay, Peter and Dias, Marcio Vinicius Bertacine (2022) Crystal structure of BtrK, a decarboxylase involved in the (S)-4-amino-2-hydroxybutyrate (AHBA) formation during butirosin biosynthesis. Journal of Molecular Structure, 1267 . 133576. doi:10.1016/j.molstruc.2022.133576 ISSN 0022-2860.
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WRAP-Crystal-structure-BtrK-decarboxylase-S-4-amino-2-hydroxybutyrate-butirosin-2022.pdf - Accepted Version - Requires a PDF viewer. Available under License Creative Commons Attribution Non-commercial No Derivatives 4.0. Download (1722Kb) | Preview |
Official URL: https://doi.org/10.1016/j.molstruc.2022.133576
Abstract
Butirosin is an aminoglycoside that has an (S)-4-amino-2-hydroxybutyrate (AHBA) moiety capable of preventing the attack of several aminoglycoside modifying enzymes. The biosynthesis and the attachment of the AHBA to the 2-deoxystreptamine (2-DOS) involve seven enzymes that use glutamate as a precursor. BtrK is a pyridoxal-5-phosphate (PLP)-dependent enzyme and performs the decarboxylation of a glutamyl moiety tethered to the peptidyl carrier protein BtrI during the AHBA biosynthetic pathway. The structure of BtrK was solved at 1.4 Å resolution and indicated a conserved folding. The PLP is covalently linked through a Schiff base to Lys49 and performs intensive hydrogen bond interactions with active site residues that are also conserved in other members of type IV PLP-dependent enzymes. Additionally, a docking simulation indicates the possible anchoring of a substrate fragment constituted of O-S-γ-Lglutamylpantetheine-4′-phosphate. The glutamyl moiety forms a number of hydrogen bonds with the putative active site residues of BtrK. The pantetheine moiety seems to perform only a few interactions and should adopt a more flexible conformation. The description of BtrK structure contributes to the understanding of the large family of PLP-dependent enzymes and also in this crucial step during the butirosin biosynthesis.
Item Type: | Journal Article | |||||||||
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Subjects: | Q Science > QD Chemistry | |||||||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Chemistry | |||||||||
SWORD Depositor: | Library Publications Router | |||||||||
Library of Congress Subject Headings (LCSH): | Aminoglycosides, Decarboxylases, Pyridoxal phosphate, Enzymes | |||||||||
Journal or Publication Title: | Journal of Molecular Structure | |||||||||
Publisher: | Elsevier BV | |||||||||
ISSN: | 0022-2860 | |||||||||
Official Date: | 5 November 2022 | |||||||||
Dates: |
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Volume: | 1267 | |||||||||
Article Number: | 133576 | |||||||||
DOI: | 10.1016/j.molstruc.2022.133576 | |||||||||
Status: | Peer Reviewed | |||||||||
Publication Status: | Published | |||||||||
Access rights to Published version: | Restricted or Subscription Access | |||||||||
Date of first compliant deposit: | 1 August 2022 | |||||||||
Date of first compliant Open Access: | 24 June 2023 | |||||||||
RIOXX Funder/Project Grant: |
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