1ELU

COMPLEX BETWEEN THE CYSTINE C-S LYASE C-DES AND ITS REACTION PRODUCT CYSTEINE PERSULFIDE.

Summary for 1ELU

• Entry DOI: 10.2210/pdb1elu/pdb
• Related: 1ELQ
• Descriptor: L-CYSTEINE/L-CYSTINE C-S LYASE, POTASSIUM ION, 2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL)-AMINO]-PROPIONIC ACID, ... (5 entities in total)
• Functional Keywords: fes cluster biosynthesis, pyridoxal 5'-phosphate, thiocysteine, aminoacrylate, enzyme-product complex, lyase
• Biological source: Synechocystis sp.
• Total number of polymer chains: 2
• Total formula weight: 86565.05

Authors

Clausen, T.,Kaiser, J.T.,Steegborn, C.,Huber, R.,Kessler, D. (deposition date: 2000-03-14, release date: 2000-04-19, Last modification date: 2024-02-07)

Primary citation

Clausen, T.,Kaiser, J.T.,Steegborn, C.,Huber, R.,Kessler, D.
Crystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis.
Proc.Natl.Acad.Sci.USA, 97:3856-3861, 2000

PubMed Abstract: FeS clusters are versatile cofactors of a variety of proteins, but the mechanisms of their biosynthesis are still unknown. The cystine C-S lyase from Synechocystis has been identified as a participant in ferredoxin FeS cluster formation. Herein, we report on the crystal structure of the lyase and of a complex with the reaction products of cystine cleavage at 1.8- and 1.55-A resolution, respectively. The sulfur-containing product was unequivocally identified as cysteine persulfide. The reactive persulfide group is fixed by a hydrogen bond to His-114 in the center of a hydrophobic pocket and is thereby shielded from the solvent. Binding and stabilization of the cysteine persulfide represent an alternative to the generation of a protein-bound persulfide by NifS-like proteins and point to the general importance of persulfidic compounds for FeS cluster assembly.

PubMed: 10760256
DOI: 10.1073/pnas.97.8.3856

Experimental method

X-RAY DIFFRACTION (1.55 Å)