1elu: Difference between revisions
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|PDB= 1elu |SIZE=350|CAPTION= <scene name='initialview01'>1elu</scene>, resolution 1.55Å | |PDB= 1elu |SIZE=350|CAPTION= <scene name='initialview01'>1elu</scene>, resolution 1.55Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PDA:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL)-AMINO]-PROPIONIC+ACID'>PDA | |LIGAND= <scene name='pdbligand=CSS:S-MERCAPTOCYSTEINE'>CSS</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PDA:2-[(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL)-AMINO]-PROPIONIC+ACID'>PDA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1elq|1ELQ]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1elu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elu OCA], [http://www.ebi.ac.uk/pdbsum/1elu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1elu RCSB]</span> | |||
}} | }} | ||
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[[Category: Kessler, D.]] | [[Category: Kessler, D.]] | ||
[[Category: Steegborn, C.]] | [[Category: Steegborn, C.]] | ||
[[Category: aminoacrylate]] | [[Category: aminoacrylate]] | ||
[[Category: enzyme-product complex]] | [[Category: enzyme-product complex]] | ||
| Line 36: | Line 36: | ||
[[Category: thiocysteine]] | [[Category: thiocysteine]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:05:15 2008'' | ||
Revision as of 17:05, 30 March 2008
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| 1elu, resolution 1.55Å | |||||||||||||
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| Ligands: | CSS, K, PDA | ||||||||||||
| Related: | 1ELQ
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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.. 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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