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[[Image:1n8j.gif|left|200px]]


{{Structure
==Crystal Structure of AhpC with Active Site Cysteine mutated to Serine (C46S)==
|PDB= 1n8j |SIZE=350|CAPTION= <scene name='initialview01'>1n8j</scene>, resolution 2.17&Aring;
<StructureSection load='1n8j' size='340' side='right'caption='[[1n8j]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1n8j]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N8J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N8J 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]] 2.17&#8491;</td></tr>
|GENE= AhpC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=602 Salmonella typhimurium])
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n8j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n8j OCA], [https://pdbe.org/1n8j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n8j RCSB], [https://www.ebi.ac.uk/pdbsum/1n8j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n8j ProSAT]</span></td></tr>
}}
</table>
 
== Function ==
'''Crystal Structure of AhpC with Active Site Cysteine mutated to Serine (C46S)'''
[https://www.uniprot.org/uniprot/AHPC_SALTY AHPC_SALTY] Directly reduces alkyl hydroperoxides with the use of electrons donated by the 57 kDa flavoprotein alkyl hydroperoxide reductase.
 
== Evolutionary Conservation ==
 
[[Image:Consurf_key_small.gif|200px|right]]
==Overview==
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n8/1n8j_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=1n8j ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Eukaryotic 2-Cys peroxiredoxins (2-Cys Prxs) not only act as antioxidants, but also appear to regulate hydrogen peroxide-mediated signal transduction. We show that bacterial 2-Cys Prxs are much less sensitive to oxidative inactivation than are eukaryotic 2-Cys Prxs. By identifying two sequence motifs unique to the sensitive 2-Cys Prxs and comparing the crystal structure of a bacterial 2-Cys Prx at 2.2 angstrom resolution with other Prx structures, we define the structural origins of sensitivity. We suggest this adaptation allows 2-Cys Prxs to act as floodgates, keeping resting levels of hydrogen peroxide low, while permitting higher levels during signal transduction.
Eukaryotic 2-Cys peroxiredoxins (2-Cys Prxs) not only act as antioxidants, but also appear to regulate hydrogen peroxide-mediated signal transduction. We show that bacterial 2-Cys Prxs are much less sensitive to oxidative inactivation than are eukaryotic 2-Cys Prxs. By identifying two sequence motifs unique to the sensitive 2-Cys Prxs and comparing the crystal structure of a bacterial 2-Cys Prx at 2.2 angstrom resolution with other Prx structures, we define the structural origins of sensitivity. We suggest this adaptation allows 2-Cys Prxs to act as floodgates, keeping resting levels of hydrogen peroxide low, while permitting higher levels during signal transduction.


==About this Structure==
Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling.,Wood ZA, Poole LB, Karplus PA Science. 2003 Apr 25;300(5619):650-3. PMID:12714747<ref>PMID:12714747</ref>
1N8J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N8J OCA].
 
==Reference==
Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling., Wood ZA, Poole LB, Karplus PA, Science. 2003 Apr 25;300(5619):650-3. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12714747 12714747]
[[Category: Salmonella typhimurium]]
[[Category: Single protein]]
[[Category: Karplus, P A.]]
[[Category: Poole, L B.]]
[[Category: Wood, Z A.]]
[[Category: ahpc]]
[[Category: ahpf]]
[[Category: alkylhydroperoxide reductase]]
[[Category: antioxidant]]
[[Category: decamer]]
[[Category: peroxidase]]
[[Category: peroxiredoxin]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:53:36 2008''
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1n8j" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Karplus PA]]
[[Category: Poole LB]]
[[Category: Wood ZA]]
Retrieved from "https://proteopedia.org/1n8j"