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Structural characterization of the hypothetical protein Lpg2622, a new member of the C1 family peptidases from Legionella pneumophila.

  • 【作者】Gong, Xiaojian,Zhao, Xiaolei,Zhang, Wei,Wang, Jinzhao,Chen, Xiaofang,Hameed, Muhammad Fazal,Zhang, Nannan,Ge, Honghua
  • 【刊名】FEBS Letters
  • 【作者单位】1 School of Life Sciences, Anhui University, Hefei, China 2 Institute of Physical Science and Information Technology, Anhui University, Hefei, China 3 School of Chemistry and Chemical Engineering, Anhui University, Hefei, China 4 Department of Biology, Taiyuan Normal University, China
  • 【年份】2018
  • 【卷号】Vol.592 No.16
  • 【页码】2798-2810
  • 【ISSN】0014-5793
  • 【关键词】LEGIONELLA pneumophila *CYSTEINE proteinase inhibitors *PEPTIDASE *PROTEIN folding *HAIRPIN *BACTERIAL growth 
  • 【摘要】 The Legionella pneumophila type II secretion system can promote bacterial growth under a wide variety of conditions and mediates the secretion of more than 25 proteins, including the uncharacterized effector Lpg2622. Here, we determined the crystal s...
  • 【文献类型】 期刊
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