ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012
Purification, crystallization and preliminary crystallographic analysis of human cystathionine β-synthase.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Disease-causing cystathionine β-synthase linker mutations impair allosteric regulation.The Journal of biological chemistry · 2023Article
- Structural insight into the unique conformation of cystathionine β-synthase fromComputational and structural biotechnology journal · 2021Article
- Screening of Heteroaromatic Scaffolds against Cystathionine Beta-Synthase Enables Identification of Substituted Pyrazolo[3,4-c]Pyridines as Potent and Selective Orthosteric Inhibitors.Molecules (Basel, Switzerland) · 2020Article
- Inter-domain communication of human cystathionine β-synthase: structural basis of S-adenosyl-L-methionine activation.The Journal of biological chemistry · 2014Article
- Structural insight into the molecular mechanism of allosteric activation of human cystathionine β-synthase by S-adenosylmethionine.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Structural basis of regulation and oligomerization of human cystathionine β-synthase, the central enzyme of transsulfuration.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Human cystathionine β-synthase (CBS) is a pyridoxal-5'-phosphate-dependent hemeprotein, whose catalytic activity is regulated by S-adenosylmethionine. CBS catalyzes the β-replacement reaction of homocysteine (Hcy) with serine to yield cystathionine. CBS is a key regulator of plasma levels of the thrombogenic Hcy and deficiency in CBS is the single most common cause of homocystinuria, an inherited metabolic disorder of sulfur amino acids. The properties of CBS enzymes, such as domain organization, oligomerization degree or regulatory mechanisms, are not conserved across the eukaryotes. The current body of knowledge is insufficient to understand these differences and their impact on CBS function and physiology. To overcome this deficiency, we have addressed the crystallization and preliminary crystallographic analysis of a protein construct (hCBS516-525) that contains the full-length CBS from Homo sapiens (hCBS) and just lacks amino-acid residues 516-525, which are located in a disordered loop. The human enzyme yielded crystals belonging to space group I222, with unit-cell parameters a=124.98, b=136.33, c=169.83 Å and diffracting X-rays to a resolution of 3.0 Å. The crystal structure appears to contain two molecules in the asymmetric unit which presumably correspond to a dimeric form of the enzyme.
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