Pal power: Demonstration of the functional association of the <i>Helicobacter pylori</i> flagellar motor with peptidoglycan-associated lipoprotein (Pal) and its preliminary crystallographic analysis
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- Zhou Xiaotian
- Department of Microbiology, Infection and Immunity Program, Monash Biomedicine Discovery Institute, Monash University, Melbourne, Victoria, Australia.
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- Rahman Mohammad M.
- Department of Microbiology, Infection and Immunity Program, Monash Biomedicine Discovery Institute, Monash University, Melbourne, Victoria, Australia.
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- Bonny Sharmin Q.
- Department of Microbiology, Infection and Immunity Program, Monash Biomedicine Discovery Institute, Monash University, Melbourne, Victoria, Australia.
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- Xin Yue
- Department of Microbiology, Infection and Immunity Program, Monash Biomedicine Discovery Institute, Monash University, Melbourne, Victoria, Australia.
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- Liddelow Nikki
- Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Victoria, Australia.
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- Khan Mohammad F.
- Department of Microbiology, Infection and Immunity Program, Monash Biomedicine Discovery Institute, Monash University, Melbourne, Victoria, Australia.
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- Tikhomirova Alexandra
- Department of Microbiology, Infection and Immunity Program, Monash Biomedicine Discovery Institute, Monash University, Melbourne, Victoria, Australia.
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- Homman-Ludiye Jihane
- Monash Micro Imaging, Biomedicine Discovery Institute, Monash University, Melbourne, Victoria, Australia.
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- Roujeinikova Anna
- Department of Microbiology, Infection and Immunity Program, Monash Biomedicine Discovery Institute, Monash University, Melbourne, Victoria, Australia. Department of Biochemistry and Molecular Biology, Monash University, Melbourne, Victoria, Australia.
抄録
<p>The bacterial flagellar motor is a molecular nanomachine, the assembly and regulation of which requires many accessory proteins. Their identity, structure and function are often discovered through characterisation of mutants with impaired motility. Here, we demonstrate the functional association of the Helicobacter pylori peptidoglycan-associated lipoprotein (HpPal) with the flagellar motor by analysing the motility phenotype of the ∆pal mutant, and present the results of the preliminary X-ray crystallographic analysis of its globular C-terminal domain HpPal-C. Purified HpPal-C behaved as a dimer in solution. Crystals of HpPal-C were grown by the hanging drop vapour diffusion method using medium molecular weight polyethylene glycol (PEG) Smear as the precipitating agent. The crystals belong to the primitive orthorhombic space group P1 with unit cell parameters a = 50.7, b = 63.0, c = 75.1 Å. X-ray diffraction data were collected to 1.8 Å resolution on the Australian Synchrotron beamline MX2. Calculation of the Matthews coefficient (VM=2.24 Å3/Da) and molecular replacement showed that the asymmetric unit contains two protein subunits. This study is an important step towards elucidation of the non-canonical role of H. pylori Pal in the regulation, or function of, the flagellar motor. </p>
収録刊行物
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- BioScience Trends
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BioScience Trends 17 (6), 491-498, 2023-12-31
特定非営利活動法人 バイオ＆ソーシャル・サイエンス推進国際研究交流会