This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2f9s

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:13, 24 February 2021) (edit) (undo)
 
(10 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2f9s.gif|left|200px]]
 
-
<!--
+
==2nd Crystal Structure Of A Soluble Domain Of ResA In The Oxidised Form==
-
The line below this paragraph, containing "STRUCTURE_2f9s", creates the "Structure Box" on the page.
+
<StructureSection load='2f9s' size='340' side='right'caption='[[2f9s]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2f9s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F9S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F9S FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-
-->
+
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1st9|1st9]], [[1su9|1su9]]</div></td></tr>
-
{{STRUCTURE_2f9s| PDB=2f9s | SCENE= }}
+
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">resa ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f9s OCA], [https://pdbe.org/2f9s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f9s RCSB], [https://www.ebi.ac.uk/pdbsum/2f9s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f9s ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[[https://www.uniprot.org/uniprot/RESA_BACSU RESA_BACSU]] Thiol-disulfide oxidoreductase which is required in disulfide reduction during c-type cytochrome synthesis. May accept reducing equivalents from CcdA, leading to breakage of disulfide bonds in apocytochrome c; following this reduction heme can be covalently attached. Does not play a role in sporulation.<ref>PMID:12637552</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f9/2f9s_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2f9s ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
'''2nd Crystal Structure Of A Soluble Domain Of ResA In The Oxidised Form'''
+
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<ref>PMID:16537372</ref>
-
 
+
-
 
+
-
==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==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
2F9S is a [[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].
+
</div>
 +
<div class="pdbe-citations 2f9s" style="background-color:#fffaf0;"></div>
-
==Reference==
+
==See Also==
-
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:[http://www.ncbi.nlm.nih.gov/pubmed/16537372 16537372]
+
*[[Protein disulfide oxidoreductase|Protein disulfide oxidoreductase]]
-
[[Category: Bacillus subtilis]]
+
== References ==
-
[[Category: Single protein]]
+
<references/>
-
[[Category: Colbert, C L.]]
+
__TOC__
-
[[Category: Deisenhofer, J.]]
+
</StructureSection>
-
[[Category: Erbel, P J.A.]]
+
[[Category: Vibrio subtilis ehrenberg 1835]]
-
[[Category: Gardner, K H.]]
+
[[Category: Large Structures]]
-
[[Category: Wu, Q.]]
+
[[Category: Colbert, C L]]
 +
[[Category: Deisenhofer, J]]
 +
[[Category: Erbel, P J.A]]
 +
[[Category: Gardner, K H]]
 +
[[Category: Wu, Q]]
 +
[[Category: Oxidoreductase]]
[[Category: Thioredoxin-like protein]]
[[Category: Thioredoxin-like protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:38:25 2008''
 

Current revision

2nd Crystal Structure Of A Soluble Domain Of ResA In The Oxidised Form

PDB ID 2f9s

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2f9s"
Personal tools