Abstract：
Itaconyl-CoA hydratase in Pseudomonas aeruginosa (PaIch) converts itaconyl-CoA to (S)-citramalyl-CoA upon addition of a water molecule, a part of an itaconate catabolic pathway in virulent organisms required for their survival in humans host cells. Crystal structure analysis of PaIch showed that a unique N-terminal hotdog fold containing a 4-residue short helical segment α3-, named as an \"eaten sausage\", followed by a flexible loop region slipped away from the conserved β-sheet scaffold, whereas the C-terminal hotdog fold is similar to all MaoC. A conserved hydratase motif with catalytic residues provides mechanistic insights into catalysis, and existence of a longer substrate binding tunnel may suggest the binding of longer CoA derivatives.
摘要：
铜绿假单胞菌（PaIch）中的衣康酰CoA水合酶在添加水分子后将衣康酰CoA转化为（S）-citramalyl-CoA，毒性生物中衣康酸酯分解代谢途径的一部分，是它们在人类宿主细胞中存活所必需的。PaIch的晶体结构分析表明，独特的N末端热狗褶皱包含4残基的短螺旋段α3-，名为“吃香肠”，随后是一个柔性环区域从保守的β-折叠支架上滑落，而C端热狗褶皱与所有MaoC相似。具有催化残基的保守水合酶基序提供了对催化的机理见解，和更长的底物结合隧道的存在可能表明更长的CoA衍生物的结合。
