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X-ray Structure of Catenated Lytic Transglycosylase SltB1
Biochemistry ( IF 2.9 ) Pub Date : 2017-11-16 00:00:00 , DOI: 10.1021/acs.biochem.7b00932
Teresa Domínguez-Gil 1 , Rafael Molina 1 , David A. Dik 2 , Edward Spink 2 , Shahriar Mobashery 2 , Juan A. Hermoso 1
Affiliation  

Formation of catenanes by proteins is rare, with few known examples. We report herein the X-ray structure of a catenane dimer of lytic transglycosylase SltB1 of Pseudomonas aeruginosa. The enzyme is soluble and exists in the periplasmic space, where it modifies the bacterial cell wall. The catenane dimer exhibits the protein monomers in a noncovalent chain-link arrangement, whereby a stretch of 51 amino acids (to become a loop and three helices) from one monomer threads through the central opening of the structure of the partner monomer. The protein folds after threading in a manner that leaves two helices (α1 and α2) as stoppers to impart stability to the dimer structure. The symmetric embrace by the two SltB1 molecules occludes both active sites entirely, an arrangement that is sustained by six electrostatic interactions between the two monomers. In light of the observation of these structural motifs in all members of Family 3 lytic transglycosylases, catenanes might be present for those enzymes, as well. The dimeric catenane might represent a regulated form of SltB1.

中文翻译:

链状裂解性糖基转移糖基转移酶SltB1的X射线结构

蛋白质形成链环的情况很少见,很少有已知的例子。我们在这里报告铜绿假单胞菌的裂解转糖基化酶SltB1的链烷二聚体的X射线结构。该酶是可溶的,存在于周质空间,在此修饰细菌细胞壁。链烷二聚体以非共价链键排列显示蛋白质单体,由此从一个单体延伸出51个氨基酸(成为一个环和三个螺旋)的氨基酸穿过配对单体结构的中心开口。蛋白质在穿线后折叠,留下两个螺旋(α1和α2)作为终止子,为二聚体结构赋予稳定性。两个SltB1分子的对称包围完全封闭了两个活性位点,这种排列由两个单体之间的六次静电相互作用所维持。鉴于在家族3的裂解转糖基化酶的所有成员中观察到这些结构基序,这些酶也可能存在连环烷。
更新日期:2017-11-17
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