SELENO-METHIONINE CAE

点击翻译按钮获取中文摘要

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.