非青霉素结合模块的E-46-D-160多肽片段对迟缓肠球菌低亲和力、多模块B类青霉素结合蛋白5折叠的重要性。
Importance of the E-46-D-160 polypeptide segment of the non-penicillin-binding module for the folding of the low-affinity, multimodular class B penicillin-binding protein 5 of Enterococus hirae.
作者信息
Mollerach M E, Partoune P, Coyette J, Ghuysen J M
机构信息
Centre d'Ingénierie des Protéines, Institut de Chimie, Université de Liège, Belgium.
出版信息
J Bacteriol. 1996 Mar;178(6):1774-5. doi: 10.1128/jb.178.6.1774-1775.1996.
Abstract
Compared with the other class B multimodular penicillin- binding proteins (PBPs), the low-affinity PBP5 responsible for penicillin resistance in Enterococcus hirae R40, has an extended non-penicillin-binding module because of the presence of an approximately 110-amino-acid E-46(-)D-160 insert downstream from the membrane anchor. Expression of pbp5 genes lacking various parts of the insert-encoding region gives rise to proteins that are inert in terms of penicillin binding, showing that during folding of the PBP, the insert plays a role in the acquisition of a correct penicillin-binding configuration by the G-364(-)Q-678 carboxy-terminal module.
摘要
与其他B类多模块青霉素结合蛋白（PBPs）相比，负责平肠球菌R40青霉素抗性的低亲和力PBP5具有一个延伸的非青霉素结合模块，这是因为在膜锚定下游存在一个约110个氨基酸的E-46（-）D-160插入序列。缺乏插入编码区不同部分的pbp5基因的表达产生了在青霉素结合方面无活性的蛋白质，这表明在PBP折叠过程中，该插入序列在G-364（-）Q-678羧基末端模块获得正确的青霉素结合构型中发挥作用。
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