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1elu
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(New page: 200px<br /><applet load="1elu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1elu, resolution 1.55Å" /> '''COMPLEX BETWEEN THE ...)
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Revision as of 20:22, 24 November 2007
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COMPLEX BETWEEN THE CYSTINE C-S LYASE C-DES AND ITS REACTION PRODUCT CYSTEINE PERSULFIDE.
Overview
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.
About this Structure
1ELU is a Single protein structure of sequence from Synechocystis sp. with K, PDA and CSS as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the cystine C-S lyase from Synechocystis: stabilization of cysteine persulfide for FeS cluster biosynthesis., Clausen T, Kaiser JT, Steegborn C, Huber R, Kessler D, Proc Natl Acad Sci U S A. 2000 Apr 11;97(8):3856-61. PMID:10760256
Page seeded by OCA on Sat Nov 24 22:29:45 2007
