STRUCTURE OF PROLYL-4-HYDROXYLASE FROM BACILLUS ANTHRACIS

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 胶原蛋白脯氨基-4-羟基酶(P4H)是胶原生物合成过程中的一种重要酶，P4H功能障碍与纤维化疾病密切相关。唯一可用的结构是人类酶的100个氨基酸片段，由底物结合结构域组成(总共517个氨基酸)。目前还不存在包括负责结合铁和α-酮戊二酸的催化结构域的结构。我们的晶体含有全长的炭疽芽孢杆菌，有望阐明其活性机制。我们已经使用P4H的本地来源收集了完整的数据集。由于这是一种新的结构，没有已知的类似结构，分子置换不是结构确定的选择。

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. Collagen prolyl-4-hydroxylase (P4H) is an essential enzyme in collagen biosynthesis and disruption of P4H function is known to contribute to fibrotic diseases. The only structure available is a 100 amino acid fragment of the human enzyme consisting of the substrate binding domain (out of 517 amino acids total). No structures currently exist that include the catalytic domain responsible for binding both iron and alpha-ketoglutarate. Our crystals contain the full-length Bacillus anthracis and are expected to elucidate the mechanism of activity. We have collected a complete data set using a home source for P4H. Since this is a novel structure with no similar structures known, molecular replacement is not an option for structure determination.