View source for 5y63


==Crystal structure of Enterococcus faecalis AhpC==
<StructureSection load='5y63' size='340' side='right'caption='[[5y63]], [[Resolution|resolution]] 2.87&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5y63]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis_V583 Enterococcus faecalis V583]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y63 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.87&#8491;</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=5y63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y63 OCA], [https://pdbe.org/5y63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y63 RCSB], [https://www.ebi.ac.uk/pdbsum/5y63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y63 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H7C7A0_ENTFA H7C7A0_ENTFA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Enterococcus faecalis alkyl hydroperoxide reductase complex (AhpR) with its subunits AhpC (EfAhpC) and AhpF (EfAhpF) are of paramount importance to restore redox homeostasis. Recently, the novel phenomenon of swapping of the catalytic domains of EfAhpF was uncovered. Here, we visualized its counterpart EfAhpC (187 residues) from the vancomycin-resistant E. faecalis (V583) bacterium by electron microscopy and demonstrate, that in contrast to other bacterial AhpCs, EfAhpC forms a stable decamer-ring irrespective of the redox state. The first crystallographic structure (2.8A resolution) of the C-terminal truncated form (EfAhpC1-172) confirms the decamer ring and provides new insight into a transition state in-between a fully folded to a locally unfolded conformation in the catalytic center due to redox modulation. Amino acid substitutions of residues in the N- and C-termini as well as the oligomeric interphase of EfAhpC provide information into their structural and enzymatic roles. Mutagenesis, enzymatic and biophysical studies reveal the effect of the unusual existence of four cysteines in EfAhpC, which might optimize the functional adaptation of the E. faecalis enzyme under various physiological conditions.

Atomic structure and enzymatic insights into the vancomycin-resistant Enterococcus faecalis (V583) alkylhydroperoxide reductase subunit C.,Pan A, Balakrishna AM, Nartey W, Kohlmeier A, Dip PV, Bhushan S, Gruber G Free Radic Biol Med. 2017 Dec 6;115:252-265. doi:, 10.1016/j.freeradbiomed.2017.12.003. PMID:29223533<ref>PMID:29223533</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5y63" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Enterococcus faecalis V583]]
[[Category: Large Structures]]
[[Category: Balakrishna AM]]
[[Category: Grueber G]]
[[Category: Pan A]]