STRUCTURE OF PROLYL-4-HYDROXYLASE FROM BACILLUS ANTHRACIS

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目和 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 胶原蛋白脯氨酰 4-羟化酶 (P4H) 是胶原蛋白生物合成中的必需酶，已知 P4H 功能的破坏会导致纤维化疾病。 唯一可用的结构是由底物结合结构域组成的人类酶的 100 个氨基酸片段（总共 517 个氨基酸）。 目前不存在包含负责结合铁和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，有望阐明其活性机制。 我们使用 P4H 的家庭来源收集了完整的数据集。 由于这是一种新颖的结构，没有已知的类似结构，因此分子替换不是结构测定的选择。

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.