SELENO-METHIONINE CAE

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。 卤酸脱卤酶(HAD)超家族是由结构上同源的酶组成的，它们的活性部位有几个保守的序列基序。大多数HAD成员是磷酸水解酶，根据不同可分为三个亚类 在域组织上。在I类和II类中，可移动的“帽”结构域在底物结合时重新定向，将活性中心关闭到主体溶剂。第三类的成员没有这个额外的域。它是帽结构域似乎负责底物特异性。我的研究重点是了解这第三类缺乏帽结构域的酶如何能够识别不同的靶标。蛋白质CAE属于这第三类酶。它是一种功能未知的“无钙蛋白”，通过系统发育分析，似乎处于I类和III类HAD成员之间的十字路口。无囊CAE的结构将为这一超家族是如何进化的提供线索，并为III型HAD成员的底物特异性提供洞察。

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. The haloacid dehalogenase (HAD) superfamily is comprised of structurally homologous enzymes that share several conserved sequence motifs in their active site. The majority of HAD members are phosphohydrolases and may be divided into three subclasses depending on domain organization. In classes I and II, a mobile "cap" domain reorients upon substrate binding, closing the active site to bulk solvent. Members of the third class lack this additional domain. It is the cap domain that appears to be responsible for substrate specificity. My research has focused on understanding how this third class of enzymes that lacks the cap domain is able to recognize different targets. Protein CAE belongs to this third class of enzymes. It is a "capless" protein with unknown function that by phylogenetic analysis, appears to be at the cross roads between class I and III HAD members. The structure of capless CAE will provide clues as to how this superfamily has evolved as well as providing insight to substrate specificity of the type III HAD members.