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2h1d

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Revision as of 08:04, 18 October 2017

ResA pH 9.25

Structural highlights

2h1d is a 2 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1su9, 1st9, 2h19, 2h1a, 2h1b, 2h1g
Gene:	resA ("Bacillus globigii" Migula 1900)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

ResA, an extracytoplasmic thioredoxin from Bacillus subtilis, acts in cytochrome c maturation by reducing the disulfide bond present in apocytochromes prior to covalent attachment of heme. This reaction is (and has to be) specific, as broad substrate specificity would result in unproductive shortcircuiting with the general oxidizing thioredoxin(s) present in the same compartment. Using mutational analysis and subsequent biochemical and structural characterization of active site variants, we show that reduced ResA displays unusually low reactivity at neutral pH, consistent with the observed high pKa values>8 for both active site cysteines. Residue Glu80 is shown to play a key role in controlling the acid-base properties of the active site. A model in which substrate binding dramatically enhances the reactivity of the active site cysteines is proposed to account for the specificity of the protein. Such a substratemediated activation mechanism is likely to have wide relevance for extracytoplasmic thioredoxins.

Molecular basis for specificity of the extracytoplasmic thioredoxin ResA.,Lewin A, Crow A, Oubrie A, Le Brun NE J Biol Chem. 2006 Nov 17;281(46):35467-77. Epub 2006 Sep 13. PMID:16971393^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Erlendsson LS, Acheson RM, Hederstedt L, Le Brun NE. Bacillus subtilis ResA is a thiol-disulfide oxidoreductase involved in cytochrome c synthesis. J Biol Chem. 2003 May 16;278(20):17852-8. Epub 2003 Mar 7. PMID:12637552 doi:http://dx.doi.org/10.1074/jbc.M300103200
↑ Lewin A, Crow A, Oubrie A, Le Brun NE. Molecular basis for specificity of the extracytoplasmic thioredoxin ResA. J Biol Chem. 2006 Nov 17;281(46):35467-77. Epub 2006 Sep 13. PMID:16971393 doi:10.1074/jbc.M607047200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2h1d"

@@ Line 1: / Line 1: @@
 ==ResA pH 9.25==
 <StructureSection load='2h1d' size='340' side='right' caption='[[2h1d]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1su9|1su9]], [[1st9|1st9]], [[2h19|2h19]], [[2h1a|2h1a]], [[2h1b|2h1b]], [[2h1g|2h1g]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">resA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Bacillus globigii" Migula 1900])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1d OCA], [http://pdbe.org/2h1d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h1d RCSB], [http://www.ebi.ac.uk/pdbsum/2h1d PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1d OCA], [http://pdbe.org/2h1d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h1d RCSB], [http://www.ebi.ac.uk/pdbsum/2h1d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2h1d ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=2h1d ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 2h1d" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Protein disulfide oxidoreductase|Protein disulfide oxidoreductase]]
 == References ==
 <references/>

2h1d

From Proteopedia

Revision as of 08:04, 18 October 2017

ResA pH 9.25

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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