Mann Greg, Koehnke Jesko, Bent Andrew F, Graham Rachael, Houssen Wael, Jaspars Marcel, Schwarz-Linek Uli, Naismith James H
Biomedical Sciences Research Complex, University of St Andrews, North Haugh, St Andrews, Fife KY16 8ST, Scotland.
Marine Biodiscovery Centre, Department of Chemistry, University of Aberdeen, Meston Walk, Aberdeen AB24 3UE, Scotland.
Acta Crystallogr F Struct Biol Commun. 2014 Dec 1;70(Pt 12):1597-603. doi: 10.1107/S2053230X1402425X. Epub 2014 Nov 14.
Patellamides are members of the cyanobactin family of ribosomally synthesized and post-translationally modified cyclic peptide natural products, many of which, including some patellamides, are biologically active. A detailed mechanistic understanding of the biosynthetic pathway would enable the construction of a biotechnological `toolkit' to make novel analogues of patellamides that are not found in nature. All but two of the protein domains involved in patellamide biosynthesis have been characterized. The two domains of unknown function (DUFs) are homologous to each other and are found at the C-termini of the multi-domain proteins PatA and PatG. The domain sequence is found in all cyanobactin-biosynthetic pathways characterized to date, implying a functional role in cyanobactin biosynthesis. Here, the crystal structure of the PatG DUF domain is reported and its binding interactions with plausible substrates are investigated.
髌骨酰胺是核糖体合成并经翻译后修饰的环肽天然产物蓝细菌素家族的成员，其中许多（包括一些髌骨酰胺）具有生物活性。对生物合成途径进行详细的机理研究将有助于构建一个生物技术“工具包”，以制造自然界中不存在的新型髌骨酰胺类似物。参与髌骨酰胺生物合成的蛋白质结构域中，除两个结构域外，其余均已得到表征。这两个功能未知的结构域（DUF）彼此同源，位于多结构域蛋白PatA和PatG的C末端。该结构域序列存在于迄今已表征的所有蓝细菌素生物合成途径中，这意味着其在蓝细菌素生物合成中具有功能性作用。在此，报道了PatG DUF结构域的晶体结构，并研究了它与可能底物的结合相互作用。
