1elq
From Proteopedia
(New page: 200px<br /><applet load="1elq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1elq, resolution 1.80Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1elq.gif|left|200px]]<br /><applet load="1elq" size=" | + | [[Image:1elq.gif|left|200px]]<br /><applet load="1elq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1elq, resolution 1.80Å" /> | caption="1elq, resolution 1.80Å" /> | ||
'''CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES'''<br /> | '''CRYSTAL STRUCTURE OF THE CYSTINE C-S LYASE C-DES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | FeS clusters are versatile cofactors of a variety of proteins, but the | + | 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== | ||
| - | 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:// | + | 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.]] | ||
| - | [[Category: Kaiser, J | + | [[Category: Kaiser, J T.]] |
[[Category: Kessler, D.]] | [[Category: Kessler, D.]] | ||
[[Category: Steegborn, C.]] | [[Category: Steegborn, C.]] | ||
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[[Category: thiocysteine]] | [[Category: thiocysteine]] | ||
| - | ''Page seeded by [http:// | + | ''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
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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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