5H29

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

Summary for 5H29

• Entry DOI: 10.2210/pdb5h29/pdb
• Related: 4O5Q
• Descriptor: Thioredoxin reductase/glutathione-related protein, SULFATE ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total)
• Functional Keywords: oxidoreductase, electron donor, thioredoxin fold, fad binding
• Biological source: Enterococcus faecalis
• Total number of polymer chains: 1
• Total formula weight: 24619.68

Authors

Balakrishna, A.M.,Kwang, T.Y.,Gruber, G. (deposition date: 2016-10-14, release date: 2017-11-22, Last modification date: 2024-11-06)

Primary citation

Toh, Y.K.,Balakrishna, A.M.,Manimekalai, M.S.S.,Chionh, B.B.,Seetharaman, R.R.C.,Eisenhaber, F.,Eisenhaber, B.,Gruber, G.
Novel insights into the vancomycin-resistant Enterococcus faecalis (V583) alkylhydroperoxide reductase subunit F
Biochim. Biophys. Acta, 1861:3201-3214, 2017

PubMed Abstract: 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 2.3Å resolution structure of the NTD_N/C domain reveals a unique loop-helix stretch (ILKDTEPAKELLYGIEKM) not present in homologue domains of other prokaryotic AhpFs. Deletion of the unique PAKELLY-helix or of PAKELL 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.

PubMed: 28935609
DOI: 10.1016/j.bbagen.2017.09.011

Experimental method

X-RAY DIFFRACTION (2.3 Å)