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Open AccessArticle

Crystal Structure of Bacterial Cystathionine Γ-Lyase in The Cysteine Biosynthesis Pathway of Staphylococcus aureus

1
Department of Agricultural Biotechnology, Center for Food Safety and Toxicology, Center for Food and Bioconvergence, Research Institute for Agriculture and Life Sciences, Seoul National University, Seoul 08826, Korea
2
Department of Beauty Care Industry, College of Medical Science, Deagu Haany University, Gyeongsan, Gyeongbuk 38610, Korea
*
Authors to whom correspondence should be addressed.
Crystals 2019, 9(12), 656; https://doi.org/10.3390/cryst9120656
Received: 17 October 2019 / Revised: 4 December 2019 / Accepted: 5 December 2019 / Published: 9 December 2019
(This article belongs to the Special Issue Crystallographic Studies of Enzymes)
Many enzymes require pyridoxal 5’-phosphate (PLP) as an essential cofactor and share active site residues in mediating diverse enzymatic reactions. Methionine can be converted into cysteine by cystathionine γ-lyases (CGLs) through a transsulfuration reaction dependent on PLP. In bacteria, MccB, also known as YhrB, exhibits CGL activity that cleaves the C–S bond of cystathionine at the γ position. In this study, we determined the crystal structure of MccB from Staphylococcus aureus in its apo- and PLP-bound forms. The structures of MccB exhibited similar molecular arrangements to those of MetC-mediating β-elimination with the same substrate and further illustrated PLP-induced structural changes in MccB. A structural comparison to MetC revealed a longer distance between the N-1 atom of the pyridine ring of PLP and the Oδ atom of the Asp residue, as well as a wider and more flexible active site environment in MccB. We also found a hydrogen bond network in Ser-water-Ser-Glu near the Schiff base nitrogen atom of the PLP molecule and propose the Ser-water-Ser-Glu motif as a general base for the γ-elimination process. Our study suggests the molecular mechanism for how homologous enzymes that use PLP as a cofactor catalyze different reactions with the same active site residues. View Full-Text
Keywords: cystathionine γ-lyases; cysteine biosynthesis; Staphylococcus aureus; pyridoxal 5’-phosphate (PLP) cystathionine γ-lyases; cysteine biosynthesis; Staphylococcus aureus; pyridoxal 5’-phosphate (PLP)
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MDPI and ACS Style

Lee, D.; Jeong, S.; Ahn, J.; Ha, N.-C.; Kwon, A.-R. Crystal Structure of Bacterial Cystathionine Γ-Lyase in The Cysteine Biosynthesis Pathway of Staphylococcus aureus. Crystals 2019, 9, 656. https://doi.org/10.3390/cryst9120656

AMA Style

Lee D, Jeong S, Ahn J, Ha N-C, Kwon A-R. Crystal Structure of Bacterial Cystathionine Γ-Lyase in The Cysteine Biosynthesis Pathway of Staphylococcus aureus. Crystals. 2019; 9(12):656. https://doi.org/10.3390/cryst9120656

Chicago/Turabian Style

Lee, Dukwon; Jeong, Soyeon; Ahn, Jinsook; Ha, Nam-Chul; Kwon, Ae-Ran. 2019. "Crystal Structure of Bacterial Cystathionine Γ-Lyase in The Cysteine Biosynthesis Pathway of Staphylococcus aureus" Crystals 9, no. 12: 656. https://doi.org/10.3390/cryst9120656

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