View source for 5h29


==Crystal Structure of the NTD_N/C domain of Alkylhydroperoxide Reductase AhpF from Enterococcus Faecalis (V583)==
<StructureSection load='5h29' size='340' side='right'caption='[[5h29]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5h29]] is a 1 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=5H29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H29 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=5h29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h29 OCA], [https://pdbe.org/5h29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h29 RCSB], [https://www.ebi.ac.uk/pdbsum/5h29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h29 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q830N9_ENTFA Q830N9_ENTFA] 
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== Publication Abstract from PubMed ==
The ability of the vancomycin-resistant Enterococcus faecalis (V583) to restore redox homeostasis via antioxidant defense mechanism is of importance, and knowledge into this defense is essential to understand its antibiotic-resistance and survival in hosts. The flavoprotein disulfide reductase AhpR, composed of the subunits AhpC and AhpF, represents one such vital part. Circular permutation was found to be a feature of the AhpF protein family. E. faecalis (V583) AhpF (EfAhpF) appears to be a representative of a minor subclass of this family, the typically N-terminal two-fold thioredoxin-like domain (NTD_N/C) is located at the C-terminus, whereas the pyridine nucleotide-disulfide oxidoreductase domain is encoded in the N-terminal part of its sequence. In EfAhpF, these two domains are connected via an unusually long linker region providing optimal communication between both domains. EfAhpF forms a dimer in solution similar to Escherichia coli AhpF. The crystallographic 2.3A resolution structure of the NTD_N/C domain reveals a unique loop-helix stretch (409ILKDTEPAKELLYGIEKM426) not present in homologue domains of other prokaryotic AhpFs. Deletion of the unique 415PAKELLY421-helix or of 415PAKELL420 affects protein stability or attenuates peroxidase activity. Furthermore, mutation of Y421 is described to be essential for E. faecalis AhpF's optimal NADH-oxidative activity.

Novel insights into the vancomycin-resistant Enterococcus faecalis (V583) alkylhydroperoxide reductase subunit F.,Toh YK, Balakrishna AM, Manimekalai MSS, Chionh BB, Seetharaman RRC, Eisenhaber F, Eisenhaber B, Gruber G Biochim Biophys Acta. 2017 Dec;1861(12):3201-3214. doi:, 10.1016/j.bbagen.2017.09.011. Epub 2017 Sep 19. PMID:28935609<ref>PMID:28935609</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5h29" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Enterococcus faecalis V583]]
[[Category: Large Structures]]
[[Category: Balakrishna AM]]
[[Category: Gruber G]]
[[Category: Kwang TY]]