Cystathionine beta-lyase
From Proteopedia
(Difference between revisions)
| Line 11: | Line 11: | ||
== Structural highlights == | == Structural highlights == | ||
| - | The structure of the EcCBL shows 3 spatially different domains. The <scene name='83/833252/Cv/3'>N-terminal domain</scene> (residues 1-60) contributes to the <scene name='83/833252/Cv/6'>tetramer formation</scene>. The <scene name='83/833252/Cv/7'>second domain</scene> (residues 61-256) binds to the PLP and the <scene name='83/833252/Cv/8'>C-terminal domain</scene> (residues 257-395). <scene name='83/833252/Cv/10'>Residue Lys210 binds to PLP</scene> and mediates the proton transfer between Cα and Sγ<ref>PMID:8831789</ref>. <scene name='83/833252/Cv/ | + | The structure of the EcCBL shows 3 spatially different domains. The <scene name='83/833252/Cv/3'>N-terminal domain</scene> (residues 1-60) contributes to the <scene name='83/833252/Cv/6'>tetramer formation</scene>. The <scene name='83/833252/Cv/7'>second domain</scene> (residues 61-256) binds to the PLP and the <scene name='83/833252/Cv/8'>C-terminal domain</scene> (residues 257-395). <scene name='83/833252/Cv/10'>Residue Lys210 binds to PLP</scene> and mediates the proton transfer between Cα and Sγ<ref>PMID:8831789</ref>. <scene name='83/833252/Cv/12'>PLP binding site</scene>. Water molecules are shown as red spheres. |
</StructureSection> | </StructureSection> | ||
==3D structures of Cystathionine β-lyase== | ==3D structures of Cystathionine β-lyase== | ||
Revision as of 12:56, 17 June 2021
| |||||||||||
3D structures of Cystathionine β-lyase
Updated on 17-June-2021
References
- ↑ Ravanel S, Job D, Douce R. Purification and properties of cystathionine beta-lyase from Arabidopsis thaliana overexpressed in Escherichia coli. Biochem J. 1996 Dec 1;320 ( Pt 2):383-92. doi: 10.1042/bj3200383. PMID:8973544 doi:http://dx.doi.org/10.1042/bj3200383
- ↑ Yamanishi T, Tuboi S. The mechanism of the L-cystine cleavage reaction catalyzed by rat liver gamma-cystathionase. J Biochem. 1981 Jun;89(6):1913-21. doi: 10.1093/oxfordjournals.jbchem.a133393. PMID:7287665 doi:http://dx.doi.org/10.1093/oxfordjournals.jbchem.a133393
- ↑ Paul BD, Sbodio JI, Xu R, Vandiver MS, Cha JY, Snowman AM, Snyder SH. Cystathionine gamma-lyase deficiency mediates neurodegeneration in Huntington's disease. Nature. 2014 May 1;509(7498):96-100. doi: 10.1038/nature13136. Epub 2014 Mar 26. PMID:24670645 doi:http://dx.doi.org/10.1038/nature13136
- ↑ Clausen T, Huber R, Laber B, Pohlenz HD, Messerschmidt A. Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A. J Mol Biol. 1996 Sep 20;262(2):202-24. PMID:8831789 doi:10.1006/jmbi.1996.0508
