2f9s
From Proteopedia
(New page: 200px<br /><applet load="2f9s" size="450" color="white" frame="true" align="right" spinBox="true" caption="2f9s, resolution 1.401Å" /> '''2nd Crystal Structu...) |
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| - | [[Image:2f9s.gif|left|200px]]<br /><applet load="2f9s" size=" | + | [[Image:2f9s.gif|left|200px]]<br /><applet load="2f9s" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2f9s, resolution 1.401Å" /> | caption="2f9s, resolution 1.401Å" /> | ||
'''2nd Crystal Structure Of A Soluble Domain Of ResA In The Oxidised Form'''<br /> | '''2nd Crystal Structure Of A Soluble Domain Of ResA In The Oxidised Form'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The covalent attachment of heme cofactors to the apo-polypeptides via | + | 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== | ==About this Structure== | ||
| - | 2F9S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http:// | + | 2F9S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F9S OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Colbert, C | + | [[Category: Colbert, C L.]] |
[[Category: Deisenhofer, J.]] | [[Category: Deisenhofer, J.]] | ||
| - | [[Category: Erbel, P | + | [[Category: Erbel, P J.A.]] |
| - | [[Category: Gardner, K | + | [[Category: Gardner, K H.]] |
[[Category: Wu, Q.]] | [[Category: Wu, Q.]] | ||
[[Category: thioredoxin-like protein]] | [[Category: thioredoxin-like protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:19:12 2008'' |
Revision as of 15:19, 21 February 2008
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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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