Cystathionine beta-lyase

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== Structural highlights ==
== Structural highlights ==
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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/9'>Residue Lys210 binds to PLP</scene> and mediates the proton transfer between Cα and Sγ<ref>PMID:8831789</ref>.
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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/11'>PLP binding site</scene>.
</StructureSection>
</StructureSection>
==3D structures of Cystathionine β-lyase==
==3D structures of Cystathionine β-lyase==

Revision as of 11:47, 9 January 2020

E. coli cystathionine β-lyase complex with PLP derivative and hepes (PDB code 4itg)

Drag the structure with the mouse to rotate

3D structures of Cystathionine β-lyase

Updated on 09-January-2020

1ibj – CBL + PLP – Arabidopsis thaliana
1cl1 – EcCBL + PLP derivative – Escherichia coli
4itg – EcCBL (mutant) + PLP derivative
1cl2 – EcCBL + aminoethoxy glycine
2fq6, 2gqn – EcCBL + inhibitor
4itx – EcCBL (mutant) + inhibitor
6cja – LpCBL + PLP-Ala + Ser – Legionella pneumophila
6cjb – LpCBL + PLP derivative

References

  1. ↑ 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
  2. ↑ 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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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