User:João Pedro de Carvalho Pereira/Sandbox 1
From Proteopedia
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== Structure == | == Structure == | ||
| - | Cystathionine gamma-lyase exhibits a tetrameric quaternary structure when bound to its ligand (PLP), and in its apo form, it can exist as both a monomer and a tetramer, with the latter being more predominant | + | Cystathionine gamma-lyase exhibits a tetrameric quaternary structure when bound to its ligand (PLP), and in its apo form, it can exist as both a monomer and a tetramer, with the latter being more predominant <ref>PMID:19019829</ref>. The monomer comprises two domains: a <scene name='97/973103/Dominio_maior_e_menor/2'>larger PLP-binding domain and a smaller domain</scene>.<br> |
The <scene name='97/973103/Dominio_maior/1'>larger domain</scene> is characterized by the presence of an alpha/beta/alpha structure, and a mixed beta-sheet surrounded by eight alpha-helices. On the other hand, the <scene name='97/973103/Dominio_menor/2'>smaller domain</scene> possesses a four-stranded antiparallel beta-sheet and three alpha-helices on one side of the beta-sheet. | The <scene name='97/973103/Dominio_maior/1'>larger domain</scene> is characterized by the presence of an alpha/beta/alpha structure, and a mixed beta-sheet surrounded by eight alpha-helices. On the other hand, the <scene name='97/973103/Dominio_menor/2'>smaller domain</scene> possesses a four-stranded antiparallel beta-sheet and three alpha-helices on one side of the beta-sheet. | ||
Revision as of 18:26, 22 June 2023
Cystathionine gamma-lyase (Homo sapiens)
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References
- ↑ Sun Q, Collins R, Huang S, Holmberg-Schiavone L, Anand GS, Tan CH, van-den-Berg S, Deng LW, Moore PK, Karlberg T, Sivaraman J. Structural basis for the inhibition mechanism of human cystathionine gamma-lyase, an enzyme responsible for the production of H(2)S. J Biol Chem. 2009 Jan 30;284(5):3076-85. Epub 2008 Nov 19. PMID:19019829 doi:http://dx.doi.org/10.1074/jbc.M805459200
