2h1a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:30, 14 February 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2h1a.gif|left|200px]]
 
-
{{Structure
+
==ResA C74A Variant==
-
|PDB= 2h1a |SIZE=350|CAPTION= <scene name='initialview01'>2h1a</scene>, resolution 2.400&Aring;
+
<StructureSection load='2h1a' size='340' side='right'caption='[[2h1a]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
+
<table><tr><td colspan='2'>[[2h1a]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H1A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H1A FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-
|GENE= resA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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=2h1a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h1a OCA], [https://pdbe.org/2h1a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h1a RCSB], [https://www.ebi.ac.uk/pdbsum/2h1a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h1a 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/h1/2h1a_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=2h1a ConSurf].
 +
<div style="clear:both"></div>
-
'''ResA C74A Variant'''
+
==See Also==
-
 
+
*[[Protein disulfide oxidoreductase 3D structures|Protein disulfide oxidoreductase 3D structures]]
-
 
+
== References ==
-
==Overview==
+
<references/>
-
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&gt;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.
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
2H1A 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=2H1A OCA].
+
-
 
+
-
==Reference==
+
-
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:[http://www.ncbi.nlm.nih.gov/pubmed/16971393 16971393]
+
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Brun, N E.Le.]]
+
[[Category: Crow A]]
-
[[Category: Crow, A.]]
+
[[Category: Le Brun NE]]
-
[[Category: Lewin, A.]]
+
[[Category: Lewin A]]
-
[[Category: Oubrie, A.]]
+
[[Category: Oubrie A]]
-
[[Category: EDO]]
+
-
[[Category: c74a]]
+
-
[[Category: mutant]]
+
-
[[Category: resa]]
+
-
[[Category: thioredoxin]]
+
-
[[Category: variant]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:11:22 2008''
+

Current revision

ResA C74A Variant

PDB ID 2h1a

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/2h1a"
Personal tools