Crystal Structure of the NTD_N/C domain of Alkylhydroperoxide Reductase AhpF from Enterococcus Faecalis (V583)Crystal Structure of the NTD_N/C domain of Alkylhydroperoxide Reductase AhpF from Enterococcus Faecalis (V583)

Structural highlights

5h29 is a 1 chain structure with sequence from Enterococcus faecalis V583. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q830N9_ENTFA

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[1]

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

References

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

5h29, resolution 2.30Å

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