与一种名为放线菌素的天然抑制剂结合的大肠杆菌肽脱甲酰基酶的1H、13C和15N核磁共振归属
1H, 13C and 15N NMR assignments of the E. coli peptide deformylase in complex with a natural inhibitor called actinonin.
作者信息
Larue Valéry, Seijo Bili, Tisne Carine, Dardel Frédéric
机构信息
UMR8015, CNRS, 75006, Paris, France.
出版信息
Biomol NMR Assign. 2009 Jun;3(1):153-5. doi: 10.1007/s12104-009-9164-6. Epub 2009 May 7.
In eubacteria, the formyl group of nascent polypeptides is removed by peptide deformylase protein (PDF). This is the reason why PDF has received special attention in the course of the search for new antibacterial agents. We observed by NMR that actinonin, a natural inhibitor, induced drastic changes in the HSQC spectrum of E. coli PDF. We report here the complete NMR chemical shift assignments of PDF resonances bound to actinonin.
在真细菌中，新生多肽的甲酰基由肽脱甲酰基酶蛋白（PDF）去除。这就是为什么在寻找新型抗菌剂的过程中，PDF受到特别关注的原因。我们通过核磁共振观察到，天然抑制剂放线菌素会导致大肠杆菌PDF的HSQC谱发生剧烈变化。我们在此报告与放线菌素结合的PDF共振的完整核磁共振化学位移归属。
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