Premium
Predicted topology of the N‐terminal domain of the hydrophilic subunit of the mannose transporter of Escherichia coli
Author(s) -
Marković-Housley Zora,
Balbach Jochen,
Stolz Beat,
Génovésio-Taverne Jean-Claude
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80138-x
Subject(s) - antiparallel (mathematics) , flavodoxin , protein subunit , chemistry , mannose , protein folding , folding (dsp implementation) , stereochemistry , crystallography , protein secondary structure , biochemistry , gene , enzyme , ferredoxin , physics , quantum mechanics , magnetic field , electrical engineering , engineering
A folding topology for the homodimeric N‐terminal domain (IIA, 2 × 14 kDa) of the hydrophilic subunit (IIAB man ) of the mannose transporter of E. coli is proposed. The prediction is based on (i) tertiary structure prediction methods, and (ii) functional properties of site‐directed mutants in correlation with NMR‐derived α/β secondary structure data. The 3D structure profile suggested that the overall fold of IIA is similar to that of the unrelated protein, flavodoxin, which is an open‐stranded parallel β‐sheet with a strand order of 5 4 3 1 2. The 3D model of IIA, constructed using the known atomic structure of flavodoxin, is consistent with the results from site‐directed mutagenesis. Recently NMR results confirmed the open parallel β‐sheet with a strand order of 4 3 12 (residues 1‐120) of our model whereas β‐strand 5 (residues 127–130) was shown to be antiparallel to β‐strand 4. The correctly predicted fold includes 90% of the monomeric subunit sequence and contains all functional sites of the IIA domain.