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1elq

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(New page: 200px<br /><applet load="1elq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1elq, resolution 1.80&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1elq.gif|left|200px]]<br /><applet load="1elq" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1elq.gif|left|200px]]<br /><applet load="1elq" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1elq, resolution 1.80&Aring;" />
caption="1elq, resolution 1.80&Aring;" />
'''CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES'''<br />
'''CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES'''<br />
==Overview==
==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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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==
==About this Structure==
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1ELQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with K and PLP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ELQ OCA].
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1ELQ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with <scene name='pdbligand=K:'>K</scene> and <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELQ OCA].
==Reference==
==Reference==
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[[Category: Clausen, T.]]
[[Category: Clausen, T.]]
[[Category: Huber, R.]]
[[Category: Huber, R.]]
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[[Category: Kaiser, J.T.]]
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[[Category: Kaiser, J T.]]
[[Category: Kessler, D.]]
[[Category: Kessler, D.]]
[[Category: Steegborn, C.]]
[[Category: Steegborn, C.]]
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[[Category: thiocysteine]]
[[Category: thiocysteine]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:29:17 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:29:09 2008''

Revision as of 10:29, 21 February 2008


1elq, resolution 1.80Å

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

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

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

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