9TCF
Crystal Structure of Cystathionine beta-Synthase from Pseudomonas aeruginosa
Summary for 9TCF
| Entry DOI | 10.2210/pdb9tcf/pdb |
| Descriptor | Cysteine synthase B, PYRIDOXAL-5'-PHOSPHATE (3 entities in total) |
| Functional Keywords | homocysteine, transsulfuration, hydrogen sulfide, cbs, cysteine, bateman, plp, cystathionine, gram negative, bacteria, multiresistent bacteria, mdr, lyase |
| Biological source | Pseudomonas aeruginosa More |
| Total number of polymer chains | 4 |
| Total formula weight | 197842.68 |
| Authors | |
| Primary citation | Conter, C.,Nunez-Franco, R.,Pietrafesa, D.,Fernandez-Rodriguez, C.,Pedretti, M.,Perbellini, E.,Mordenti, G.,Mase, N.,Dominici, P.,Majtan, T.,Falconi, M.,Martinez-Chantar, M.L.,Jimenez-Oses, G.,Astegno, A.,Martinez-Cruz, L.A. A distinct domain organization of cystathionine beta-synthase underlies cysteine and H 2 S biosynthesis in Pseudomonas aeruginosa and Klebsiella pneumoniae. Commun Biol, 2026 Cited by PubMed Abstract: Activation of the reverse transsulfuration pathway contributes to the survival and persistence of multidrug-resistant bacteria. The first step of this pathway, catalyzed by the enzyme cystathionine β-synthase (CBS), plays a crucial role in maintaining redox balance and cysteine homeostasis, making it an attractive therapeutic target against multidrug-resistant infections. In this study, we demonstrate that both Pseudomonas aeruginosa CBS and Klebsiella pneumoniae CBS exhibit high responsiveness to the allosteric activator S-adenosylmethionine (SAM) and preferentially utilize O-acetylserine (OAS) as a substrate over serine. The crystal structure of PaCBS and the AlphaFold-2 model of KpCBS reveal a novel domain organization characterized by an inverted arrangement of the regulatory Bateman module relative to the catalytic core. These findings provide a new structural and functional basis for the selective inhibition of CBS in multidrug-resistant pathogens. PubMed: 42374125DOI: 10.1038/s42003-026-10520-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.43 Å) |
Structure validation
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