In:
Proteins: Structure, Function, and Bioinformatics, Wiley, Vol. 90, No. 7 ( 2022-07), p. 1434-1442
Abstract:
Oligopeptide permease A (OppA) plays an important role in the nutrition of cells and various signaling processes. In archaea, OppA is a major protein present in membrane vesicles of Thermococcales . Because there being no crystal structures of archaeal OppAs determined to date, we report the crystal structure of archaeal OppA from Thermococcus kodakaraensi s (TkOppA) at 2.3 Å resolution by the single‐wavelength anomalous dispersion method. TkOppA consists of three domains similarly to bacterial OppAs, and the inserted regions not present in bacterial OppAs are at the periphery of the core region. An endogenous pentapeptide was bound in the pocket of domains I and III of TkOppA by hydrogen bonds of main‐chain atoms of the peptide and hydrophobic interactions. No hydrogen bonds of side‐chain atoms of the peptide were observed; thus, TkOppA may have low peptide selectivity but some preference for residues 2 and 3. TkOppA has a relatively large pocket and can bind a nonapeptide; therefore, it is suitable for the binding of large peptides similarly to OppAs of Gram‐positive bacteria.
Type of Medium:
Online Resource
ISSN:
0887-3585
,
1097-0134
Language:
English
Publisher:
Wiley
Publication Date:
2022
detail.hit.zdb_id:
1475032-6
SSG:
12
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