1elq

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{{STRUCTURE_1elq| PDB=1elq | SCENE= }}
{{STRUCTURE_1elq| PDB=1elq | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES'''
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===CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10760256 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10760256}}
==About this Structure==
==About this Structure==
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[[Category: Pyridoxal 5'-phosphate]]
[[Category: Pyridoxal 5'-phosphate]]
[[Category: Thiocysteine]]
[[Category: Thiocysteine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:57:02 2008''

Revision as of 21:57, 30 June 2008

Image:1elq.png

Template:STRUCTURE 1elq

CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES

Template:ABSTRACT PUBMED 10760256

About this Structure

1ELQ is a Single protein structure of sequence from Synechocystis sp.. 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

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