Predicted topology of the N‐terminal domain of the hydrophilic subunit of the mannose transporter of Escherichia coli

FEBS Letters

Balbach, Jochen³  Marković-Housley, Zora²  Génovésio-Taverne, Jean-Claude¹  Stolz, Beat² 

[1] Abteilung Struktwbiologie, Biozentrum der Universität Basel, CH-4056 Basel, Switzerland;Institut für Biochemie der Universität Bern, Freiestrasse 3, CH-3012 Bern, Switzerland;Organisch Chemische Institut, Technische Universität München, 85747 Garching, Germany

关键词: Mannose transporter;    α/β protein;    Protein topology;    3D structure prediction;    IIA;    amino-terminal domain of hydrophilic subunit of mannose transporter;    HPr;    histidine containing phosphoryl carrier protein;    NMR;    nuclear magnetic resonance;   

DOI  :  10.1016/0014-5793(94)80138-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown