التفاصيل البيبلوغرافية
| العنوان: |
The role of calcium binding to the EF-hand-like motif in bacterial solute-binding protein for alginate import. |
| المؤلفون: |
Kenji Okumura, Yukie Maruyama, Ryuichi Takase, Bunzo Mikami, Kousaku Murata, Wataru Hashimoto |
| المصدر: |
Bioscience, Biotechnology & Biochemistry; Dec2021, Vol. 85 Issue 12, p2410-2419, 10p |
| مصطلحات موضوعية: |
ATP-binding cassette transporters, BACTERIAL proteins, ALGINIC acid, CALCIUM, X-ray crystallography, LIPOSOMES |
| مستخلص: |
Gram-negative Sphingomonas sp. A1 incorporates acidic polysaccharide alginate into the cytoplasm via a cell-surface alginate-binding protein (AlgQ2)-dependent ATP-binding cassette transporter (AlgM1M2SS). We investigated the function of calcium bound to the EF-hand-like motif in AlgQ2 by introducing mutations at the calcium-binding site. The X-ray crystallography of the AlgQ2 mutant (D179A/E180A) demonstrated the absence of calcium binding and significant disorder of the EF-hand-like motif. Distinct from the wild-type AlgQ2, the mutant was quite unstable at temperature of strain A1 growth, although unsaturated alginate oligosaccharides stabilized the mutant by formation of substrate/protein complex. In the assay of ATPase and alginate transport by AlgM1M2SS reconstructed in the liposome, the wild-type and mutant AlgQ2 induced AlgM1M2SS ATPase activity in the presence of unsaturated alginate tetrasaccharide. These results indicate that the calcium bound to EF-hand-like motif stabilizes the substrate-unbound AlgQ2 but is not required for the complexation of substrate-bound AlgQ2 and AlgM1M2SS. [ABSTRACT FROM AUTHOR] |
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| قاعدة البيانات: |
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