6xo2

Structural Characterization of Beta Cyanoalanine Synthase from Tetranychus Urticae (two-spotted spider mite)Structural Characterization of Beta Cyanoalanine Synthase from Tetranychus Urticae (two-spotted spider mite)

Structural highlights

6xo2 is a 1 chain structure with sequence from Tetur. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	6pmu
Gene:	107363798 (TETUR)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Tetranychus urticae is a polyphagous spider mite that can feed on more than 1100 plant species including cyanogenic plants. The herbivore genome contains a horizontally acquired gene tetur10g01570 (TuCAS) that was previously shown to participate in cyanide detoxification. To understand the structure and determine the function of TuCAS in T. urticae, crystal structures of the protein with lysine conjugated pyridoxal phosphate (PLP) were determined. These structures reveal extensive TuCAS homology with the beta-substituted alanine synthase family, and they show that this enzyme utilizes a similar chemical mechanism involving a stable alpha-aminoacrylate intermediate in beta-cyanoalanine and cysteine synthesis. We demonstrate that TuCAS is more efficient in the synthesis of beta-cyanoalanine, which is a product of the detoxification reaction between cysteine and cyanide, than in the biosynthesis of cysteine. Also, the enzyme carries additional enzymatic activities that were not previously described. We show that TuCAS can detoxify cyanide using O-acetyl-L-serine as a substrate, leading to the direct formation of beta-cyanoalanine. Moreover, it catalyzes the reaction between the TuCAS-bound alpha-aminoacrylate intermediate and aromatic compounds with a thiol group. In addition, we have tested several compounds as TuCAS inhibitors. Overall, this study identifies additional functions for TuCAS and provides new molecular insight into the xenobiotic metabolism of T. urticae.

Structural and functional characterization of beta-cyanoalanine synthase from Tetranychus urticae.,Daneshian L, Renggli I, Hanaway R, Offermann LR, Schlachter CR, Hernandez Arriaza R, Henry S, Prakash R, Wybouw N, Dermauw W, Shimizu LS, Van Leeuwen T, Makris TM, Grbic V, Grbic M, Chruszcz M Insect Biochem Mol Biol. 2022 Jan 19;142:103722. doi: 10.1016/j.ibmb.2022.103722. PMID:35063675^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Daneshian L, Renggli I, Hanaway R, Offermann LR, Schlachter CR, Hernandez Arriaza R, Henry S, Prakash R, Wybouw N, Dermauw W, Shimizu LS, Van Leeuwen T, Makris TM, Grbic V, Grbic M, Chruszcz M. Structural and functional characterization of beta-cyanoalanine synthase from Tetranychus urticae. Insect Biochem Mol Biol. 2022 Jan 19;142:103722. doi: 10.1016/j.ibmb.2022.103722. PMID:35063675 doi:http://dx.doi.org/10.1016/j.ibmb.2022.103722

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OCA

[1] Daneshian L, Renggli I, Hanaway R, Offermann LR, Schlachter CR, Hernandez Arriaza R, Henry S, Prakash R, Wybouw N, Dermauw W, Shimizu LS, Van Leeuwen T, Makris TM, Grbic V, Grbic M, Chruszcz M. Structural and functional characterization of beta-cyanoalanine synthase from Tetranychus urticae. Insect Biochem Mol Biol. 2022 Jan 19;142:103722. doi: 10.1016/j.ibmb.2022.103722. PMID:35063675 doi:http://dx.doi.org/10.1016/j.ibmb.2022.103722

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