2f9s
From Proteopedia
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|PDB= 2f9s |SIZE=350|CAPTION= <scene name='initialview01'>2f9s</scene>, resolution 1.401Å | |PDB= 2f9s |SIZE=350|CAPTION= <scene name='initialview01'>2f9s</scene>, resolution 1.401Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= resa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= resa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1st9|1ST9]], [[1su9|1SU9]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f9s OCA], [http://www.ebi.ac.uk/pdbsum/2f9s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f9s RCSB]</span> | ||
}} | }} | ||
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[[Category: thioredoxin-like protein]] | [[Category: thioredoxin-like protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:59:50 2008'' |
Revision as of 23:59, 30 March 2008
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| , resolution 1.401Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | resa (Bacillus subtilis) | ||||||
| Related: | 1ST9, 1SU9
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
2nd Crystal Structure Of A Soluble Domain Of ResA In The Oxidised Form
Overview
The covalent attachment of heme cofactors to the apo-polypeptides via thioether bonds is unique to the maturation of c-type cytochromes. A number of thiol-disulfide oxidoreductases prepare the apocytochrome for heme insertion in system I and II cytochrome c maturation. Although most thiol-disulfide oxidoreductases are nonspecific, the less common, specific thiol-disulfide oxidoreductases may be key to directing the usage of electrons. Here we demonstrate that unlike other thiol-disulfide oxidoreductases, the protein responsible for reducing oxidized apocytochrome c in Bacillus subtilis, ResA, is specific for cytochrome c550 and utilizes alternate conformations to recognize redox partners. We report solution NMR evidence that ResA undergoes a redox-dependent conformational change between oxidation states, as well as data showing that ResA utilizes a surface cavity present only in the reduced state to recognize a peptide derived from cytochrome c550. Finally, we confirm that ResA is a specific thiol-disulfide oxidoreductase by comparing its reactivity to our mimetic peptide with its reactivity to oxidized glutathione, a nonspecific substrate. This study biochemically demonstrates the specificity of this thiol-disulfide oxidoreductase and enables us to outline a structural mechanism of regulating the usage of electrons in a thiol-disulfide oxidoreductase system.
About this Structure
2F9S is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Mechanism of substrate specificity in Bacillus subtilis ResA, a thioredoxin-like protein involved in cytochrome c maturation., Colbert CL, Wu Q, Erbel PJ, Gardner KH, Deisenhofer J, Proc Natl Acad Sci U S A. 2006 Mar 21;103(12):4410-5. Epub 2006 Mar 13. PMID:16537372
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