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首页> 外文期刊>Journal of bacteriology >The non-penicillin-binding module of the tripartite penicillin-binding protein 3 of Escherichia coli is required for folding and/or stability of the penicillin-binding module and the membrane-anchoring module confers cell septation activity on the folded structure.
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The non-penicillin-binding module of the tripartite penicillin-binding protein 3 of Escherichia coli is required for folding and/or stability of the penicillin-binding module and the membrane-anchoring module confers cell septation activity on the folded structure.

机译：大肠杆菌的三重青霉素结合蛋白3的非青霉素结合模块对于青霉素结合模块的折叠和/或稳定性是必需的，并且膜锚定模块赋予折叠结构上的细胞分离活性。

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The ftsI-encoded multimodular class B penicillin-binding protein 3 (PBP3) is a key element of the cell septation machinery of Escherichia coli. Altered ftsI genes were overexpressed, and the gene products were analyzed with respect to the level of production, stability, penicillin affinity, and cell septation activity. In contrast to the serine beta-lactamases and low-molecular-mass PBPs which are autonomous folding entities, the S-259-to-V-577 penicillin-binding module of M-1-to-V-577 PBP3 lacks the amino acid sequence information for correct folding. The missing piece of information is provided by the associated G-57-to-E-258 non-penicillin-binding module which functions as a noncleaved, pseudointramolecular chaperone. Key elements of the folding information reside within the motif 1-containing R-60-to-W-110 polypeptide segment and within G-188-to-D-197 motif 3 of the n-PB module. The intermodule interaction is discussed in the light of the known three-dimensional structure (at 3.5-A [0.35-nm] resolution) of the analogous class B PBP2x of Streptococcus pneumoniae (S. Pares, N. Mouz, Y. Pétillot, R. Hakenbeck, and O. Dideberg, Nature Struct. Biol. 3:284-289, 1996). Correct folding and adoption of a stable penicillin-binding conformation are necessary but not sufficient to confer cell septation activity to PBP3 in exponentially growing cells. The in vivo activity of PBP3 also depends on the M-1-to-E-56 amino-terminal module which encompasses the cytosol, the membrane, and the periplasm and which functions as a noncleaved pseudo-signal peptide.
机译：ftsI编码的多模块B类青霉素结合蛋白3（PBP3）是大肠杆菌细胞分离机制的关键要素。改变的ftsI基因过表达，并分析了基因产物的产生水平，稳定性，青霉素亲和力和细胞分离活性。与作为自主折叠实体的丝氨酸β-内酰胺酶和低分子PBP相比，M-1-to-V-577 PBP3的S-259-to-V-577青霉素结合模块缺少氨基酸正确折叠的序列信息。缺少的信息是由相关的G-57至E-258非青霉素结合模块提供的，该模块起未裂解的假分子内分子伴侣的作用。折叠信息的关键元件位于n-PB模块的包含基序1的R-60至W-110多肽片段内以及位于G-188至D-197基序3内。根据已知的三维结构（在3.5-A [0.35 nm]分辨率下）讨论肺炎链球菌B类BBP2x的模块间相互作用（S. Pares，N。Mouz，Y。Pétillot，R （Hakenbeck和O.Dideberg，Nature Struct.Biol.3：284-289，1996）。正确折叠和采用稳定的青霉素结合构象是必要的，但不足以赋予指数增长的细胞中PBP3细胞分隔活性。 PBP3的体内活性还取决于M-1-to-E-56氨基末端模块，该模块包含细胞质，膜和周质，并起未切割的伪信号肽的作用。

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