From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2nnf.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:2nnf.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2nnf| PDB=2nnf | SCENE= }} | | {{STRUCTURE_2nnf| PDB=2nnf | SCENE= }} |
| | | | |
| - | '''Structure of the sulfur carrier protein SoxY from Chlorobium limicola f thiosulfatophilum'''
| + | ===Structure of the sulfur carrier protein SoxY from Chlorobium limicola f thiosulfatophilum=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Dissimilatory oxidation of thiosulfate in the green sulfur bacterium Chlorobium limicola f. thiosulfatophilum is carried out by the ubiquitous sulfur-oxidizing (Sox) multi-enzyme system. In this system, SoxY plays a key role, functioning as the sulfur substrate-binding protein that offers its sulfur substrate, which is covalently bound to a conserved C-terminal cysteine, to another oxidizing Sox enzyme. Here, we report the crystal structures of a stand-alone SoxY protein of C. limicola f. thiosulfatophilum, solved at 2.15 A and 2.40 A resolution using X-ray diffraction data collected at 100 K and room temperature, respectively. The structure reveals a monomeric Ig-like protein, with an N-terminal alpha-helix, that oligomerizes into a tetramer via conserved contact regions between the monomers. The tetramer can be described as a dimer of dimers that exhibits one large hydrophobic contact region in each dimer and two small hydrophilic interface patches in the tetramer. At the tetramer interface patch, two conserved redox-active C-terminal cysteines form an intersubunit disulfide bridge. Intriguingly, SoxY exhibits a dimer/tetramer equilibrium that is dependent on the redox state of the cysteines and on the type of sulfur substrate component bound to them. Taken together, the dimer/tetramer equilibrium, the specific interactions between the subunits in the tetramer, and the significant conservation level of the interfaces strongly indicate that these SoxY oligomers are biologically relevant.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17327392}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17327392 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_17327392}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| | [[Category: Sox]] | | [[Category: Sox]] |
| | [[Category: Sulfur binding protein]] | | [[Category: Sulfur binding protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:40:09 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:52:41 2008'' |
Revision as of 12:52, 28 July 2008
Template:STRUCTURE 2nnf
Structure of the sulfur carrier protein SoxY from Chlorobium limicola f thiosulfatophilum
Template:ABSTRACT PUBMED 17327392
About this Structure
2NNF is a Single protein structure of sequence from Chlorobium limicola. Full crystallographic information is available from OCA.
Reference
X-ray crystallographic analysis of the sulfur carrier protein SoxY from Chlorobium limicola f. thiosulfatophilum reveals a tetrameric structure., Stout J, Van Driessche G, Savvides SN, Van Beeumen J, Protein Sci. 2007 Apr;16(4):589-601. Epub 2007 Feb 27. PMID:17327392
Page seeded by OCA on Mon Jul 28 15:52:41 2008