STRUCTURE OF PROLYL-4-HYDROXYLASE FROM BACILLUS ANTHRACIS

该子项目是利用 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来源获得主要资金， 因此可以在其他CRISP条目中表示。列出的机构是 中心，不一定是研究者的机构。 胶原蛋白脯氨酰-4-羟化酶（P4 H）是胶原蛋白生物合成中的必需酶，并且已知P4 H功能的破坏有助于纤维化疾病。 唯一可用的结构是由底物结合结构域组成的人酶的100个氨基酸片段（总共517个氨基酸）。 目前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炭疽芽孢杆菌，并有望阐明活性机制。 我们已经收集了一个完整的数据集使用家庭来源的P4 H。 由于这是一种新结构，没有已知的类似结构，因此分子置换不是结构测定的一种选择。

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.