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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >A coiled-coil motif that sequesters ions to the hydrophobic core
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A coiled-coil motif that sequesters ions to the hydrophobic core

机译：将离子螯合到疏水核的卷曲螺旋基序

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摘要

Most core residues of coiled coils are hydrophobic. Occasional polar residues are thought to lower stability, but impart structural specificity. The coiled coils of trimeric autotransporter adhesins (TAAs) are conspicuous for their large number of polar residues in position d of the core, which often leads to their prediction as natively unstructured regions. The most frequent residue, aspar-agine (N@d), can occur in runs of up to 19 consecutive heptads, frequently in the motif [I/V]xxNTxx. In the Salmonella TAA, SadA, the core asparagines form rings of interacting residues with the following threonines, grouped around a central anion. This conformation is observed generally in N@d layers from trimeric coiled coils of known structure. Attempts to impose a different register on the motif show that the asparagines orient themselves specifically into the core, even against conflicting information from flanking domains. When engineered into the GCN4 leucine zipper, N@d layers progressively destabilized the structure, but zippers with 3 N@d layers still folded at high concentration. We propose that N@d layers maintain the coiled coils of TAAs in a soluble, export-competent state during autotransport through the outer membrane. More generally, we think that polar motifs that are both periodic and conserved may often reflect special folding requirements, rather than an unstructured state of the mature proteins.
机译：盘绕线圈的大多数芯残留物是疏水的。偶尔的极性残基被认为降低了稳定性，但赋予了结构特异性。三聚体自转运粘附素（TAA）的卷曲螺旋在核的位置d中具有大量极性残基，因此非常引人注目，这常常导致它们被预测为天然非结构化区域。最常见的残基，天冬酰胺-糖精（N @ d），可出现在多达19个连续的七肽中，经常出现在[I / V] xxNTxx基序中。在沙门氏菌TAA（SadA）中，核心天冬酰胺会与以下苏氨酸形成相互作用的残基环，这些苏氨酸围绕一个中心阴离子分组。通常从已知结构的三聚体卷曲线圈的N d层中观察到这种构象。试图在基序上施加不同的配准的尝试表明，即使针对来自侧翼结构域的冲突信息，天冬酰胺也将自身专门定向于核心。当工程化到GCN4亮氨酸拉链中时，Nd层会逐渐破坏结构的稳定性，但是具有3 Nd层的拉链仍会在高浓度下折叠。我们建议N @ d层在通过外膜的自动传输过程中，将TAA的卷曲线圈保持在可溶的，具有出口能力的状态。更一般地说，我们认为周期性且保守的极性基序通常可以反映特殊的折叠要求，而不是成熟蛋白质的非结构化状态。

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    Marcus D. Hartmann; Oswin Ridderbusch; Kornelius Zeth; Reinhard Albrecht; Oli Testa; Derek N. Woolfson; Guido Sauer; Stanislaw Dunin-Horkawicz; Andrei N. Lupas; Birte Hernandez Alvarez;

  • 作者单位

    Department of Protein Evolution Max Planck Institute for Developmental Biology, 72076 Tubingen, Germany;

    Department of Protein Evolution Max Planck Institute for Developmental Biology, 72076 Tubingen, Germany;

    Department of Protein Evolution Max Planck Institute for Developmental Biology, 72076 Tubingen, Germany;

    Department of Protein Evolution Max Planck Institute for Developmental Biology, 72076 Tubingen, Germany;

    School of Chemistry, University of Bristol, Bristol B58 1TS, United Kingdom;

    School of Chemistry, University of Bristol, Bristol B58 1TS, United Kingdom Department of Biochemistry, University of Bristol, Bristol, B58 1TD,United Kingdom;

    Department of Biochemistry, University of Bristol, Bristol, B58 1TD,United Kingdom;

    Department of Protein Evolution Max Planck Institute for Developmental Biology, 72076 Tubingen, Germany;

    Department of Protein Evolution Max Planck Institute for Developmental Biology, 72076 Tubingen, Germany;

    Department of Protein Evolution Max Planck Institute for Developmental Biology, 72076 Tubingen, Germany;

  • 收录信息 美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
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  • 关键词

    ion coordination; protein export; trimeric autotransporter adhesin; polar core residues;

    机译：离子配位;蛋白质出口;三聚体自转运粘附素;极性核残基;

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