3PC3
Full length structure of cystathionine beta-synthase from Drosophila in complex with aminoacrylate
Summary for 3PC3
| Entry DOI | 10.2210/pdb3pc3/pdb |
| Related | 3PC2 3PC4 |
| Descriptor | CG1753, isoform A, PROTOPORPHYRIN IX CONTAINING FE, 2-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]ACRYLIC ACID, ... (4 entities in total) |
| Functional Keywords | cbs, synthase, plp, heme, aminoacrylate, lyase |
| Biological source | Drosophila melanogaster (Fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 58404.52 |
| Authors | Koutmos, M.,Smith, J.L. (deposition date: 2010-10-21, release date: 2010-12-01, Last modification date: 2023-09-06) |
| Primary citation | Koutmos, M.,Kabil, O.,Smith, J.L.,Banerjee, R. Structural basis for substrate activation and regulation by cystathionine beta-synthase (CBS) domains in cystathionine {beta}-synthase. Proc.Natl.Acad.Sci.USA, 107:20958-20963, 2010 Cited by PubMed Abstract: The catalytic potential for H(2)S biogenesis and homocysteine clearance converge at the active site of cystathionine β-synthase (CBS), a pyridoxal phosphate-dependent enzyme. CBS catalyzes β-replacement reactions of either serine or cysteine by homocysteine to give cystathionine and water or H(2)S, respectively. In this study, high-resolution structures of the full-length enzyme from Drosophila in which a carbanion (1.70 Å) and an aminoacrylate intermediate (1.55 Å) have been captured are reported. Electrostatic stabilization of the zwitterionic carbanion intermediate is afforded by the close positioning of an active site lysine residue that is initially used for Schiff base formation in the internal aldimine and later as a general base. Additional stabilizing interactions between active site residues and the catalytic intermediates are observed. Furthermore, the structure of the regulatory "energy-sensing" CBS domains, named after this protein, suggests a mechanism for allosteric activation by S-adenosylmethionine. PubMed: 21081698DOI: 10.1073/pnas.1011448107 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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