STRUCTURE AND MECHANISM OF YAET

这个子项目是许多利用 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 该项目的重点是确定YaeT蛋白的结构，该蛋白是YaeT复合物的中心成分，负责将蛋白质插入细菌外膜。干扰这种外膜蛋白插入机制将是抗生素开发的有效策略;就像β-内酰胺通过抑制细胞壁合成而有效一样。YaeT由嵌入外膜的C-末端β-桶和含有五个拷贝的所谓POTRA（多肽转运相关）序列基序的N-末端周质结构域组成。我们已经确定了含有4个POTRA结构域的周质YaeT片段的晶体结构。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. This project is focused on determining the structure of the YaeT protein, which is the central component of the YaeT complex responsible for insertion of proteins in the bacterial outer membrane. Interfering with this mechanism of Outer Membrane Protein insertion would be an effective strategy for antibiotic development; much like beta-lactams are effective by inhibiting cell wall synthesis. YaeT consists of a C-terminal beta-barrel embedded in the outer membrane, and an N-terminal periplasmic domain containing five copies of so-called POTRA (polypeptide-transport-associated) sequence motifs. We have determined the crystal structure of a periplasmic YaeT fragment containing 4 POTRA domains.