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crystal structure

  • Open Access
    Molecular Basis of the Versatile Regulatory Mechanism of HtrA-Type Protease AlgW from <span class="named-content genus-species" id="named-content-1">Pseudomonas aeruginosa</span>
    Research Article | Molecular Biology and Physiology
    Molecular Basis of the Versatile Regulatory Mechanism of HtrA-Type Protease AlgW from Pseudomonas aeruginosa

    HtrA-family proteases are commonly employed to sense the protein folding stress and activate the regulated intramembrane proteolysis (RIP) cascade in Gram-negative bacteria. Here, we reveal the unique dual-signal activation and dynamic regulation properties of AlgW, an HtrA-type protease triggering the AlgU stress-response pathway, which controls alginate production and mucoid conversion in...

    Tao Li, Yingjie Song, Liming Luo, Ninglin Zhao, Lihui He, Mei Kang, Changcheng Li, Yibo Zhu, Yalin Shen, Chang Zhao, Jing Yang, Qin Huang, Xingyu Mou, Zhiyong Zong, Jinliang Yang, Hong Tang, Yongxing He, Rui Bao
  • Open Access
    The Structure of the Cysteine-Rich Domain of <span class="named-content genus-species" id="named-content-1">Plasmodium falciparum</span> P113 Identifies the Location of the RH5 Binding Site
    Research Article | Host-Microbe Biology
    The Structure of the Cysteine-Rich Domain of Plasmodium falciparum P113 Identifies the Location of the RH5 Binding Site

    Malaria is a deadly infectious disease primarily caused by the parasite Plasmodium falciparum. It remains a major global health problem, and there is no highly effective vaccine. A parasite protein called RH5 is centrally involved in the invasion of host red blood cells, making it—and the other parasite proteins it interacts with—promising vaccine targets. We recently...

    Ivan Campeotto, Francis Galaway, Shahid Mehmood, Lea K. Barfod, Doris Quinkert, Vinayaka Kotraiah, Timothy W. Phares, Katherine E. Wright, Ambrosius P. Snijders, Simon J. Draper, Matthew K. Higgins, Gavin J. Wright
  • Open Access
    Molecular Deceleration Regulates Toxicant Release to Prevent Cell Damage in <span class="named-content genus-species" id="named-content-1">Pseudomonas putida</span> S16 (DSM 28022)
    Research Article | Molecular Biology and Physiology
    Molecular Deceleration Regulates Toxicant Release to Prevent Cell Damage in Pseudomonas putida S16 (DSM 28022)

    Flavin-dependent amine oxidases have received extensive attention because of their importance in drug metabolism, Parkinson’s disease, and neurotransmitter catabolism. However, the underlying molecular mechanisms remain relatively poorly understood. Here, combining the crystal structure of NicA2 (an enzyme in the first step of the bacterial nicotine degradation pathway in ...

    Hongzhi Tang, Kunzhi Zhang, Haiyang Hu, Geng Wu, Weiwei Wang, Xiongyu Zhu, Gongquan Liu, Ping Xu
  • Open Access
    Structural Analysis of an <span class="sc">l</span>-Cysteine Desulfurase from an Ssp DNA Phosphorothioation System
    Research Article | Molecular Biology and Physiology
    Structural Analysis of an l-Cysteine Desulfurase from an Ssp DNA Phosphorothioation System

    Apart from its roles in Fe-S cluster assembly, tRNA thiolation, and sulfur-containing cofactor biosynthesis, cysteine desulfurase serves as a sulfur donor in the DNA PT modification, in which a sulfur atom substitutes a nonbridging oxygen in the DNA phosphodiester backbone. The initial sulfur mobilization from l-cysteine is catalyzed by the SspA cysteine desulfurase in the SspABCD-mediated DNA PT modification...

    Liqiong Liu, Susu Jiang, Mai Xing, Chao Chen, Chongde Lai, Na Li, Guangfeng Liu, Dan Wu, Haiyan Gao, Liang Hong, Pan Tan, Shi Chen, Zixin Deng, Geng Wu, Lianrong Wang
  • Open Access
    Crystal Structure of African Swine Fever Virus dUTPase Reveals a Potential Drug Target
    Research Article | Molecular Biology and Physiology
    Crystal Structure of African Swine Fever Virus dUTPase Reveals a Potential Drug Target

    African swine fever virus (ASFV), an Asfivirus affecting pigs and wild boars with up to 100% case fatality rate, is currently rampaging throughout China and some other countries in Asia. There is an urgent need to develop therapeutic and preventive reagents against the virus. Our crystallographic and biochemical studies reveal that ASFV E165R is a member of trimeric dUTP nucleotidohydrolase (dUTPase) family that catalyzes the...

    Changyao Li, Yan Chai, Hao Song, Changjiang Weng, Jianxun Qi, Yeping Sun, George F. Gao
  • Open Access
    Sudan Ebolavirus VP35-NP Crystal Structure Reveals a Potential Target for Pan-Filovirus Treatment
    Research Article | Molecular Biology and Physiology
    Sudan Ebolavirus VP35-NP Crystal Structure Reveals a Potential Target for Pan-Filovirus Treatment

    Outbreaks of the filoviruses can be unpredictable in timing, location, and identity of the causative virus, with each of Ebola virus, Sudan virus, Bundibugyo virus, and Marburg virus reemerging in the last several years to cause human disease with 30 to 90% lethality. The 2014–2016 outbreak in particular, with nearly 30,000 patients, highlighted the ability of these viruses to emerge unexpectedly and spread rapidly. Two ebolavirus...

    Sara Landeras-Bueno, Shun-ichiro Oda, Michael J. Norris, Zhe Li Salie, Javier Guenaga, Richard T. Wyatt, Erica Ollmann Saphire
  • Open Access
    Targeting Mannitol Metabolism as an Alternative Antimicrobial Strategy Based on the Structure-Function Study of Mannitol-1-Phosphate Dehydrogenase in <span class="named-content genus-species" id="named-content-1">Staphylococcus aureus</span>
    Research Article | Molecular Biology and Physiology
    Targeting Mannitol Metabolism as an Alternative Antimicrobial Strategy Based on the Structure-Function Study of Mannitol-1-Phosphate Dehydrogenase in Staphylococcus aureus

    Due to the shortage of effective antibiotics against drug-resistant Staphylococcus aureus, new targets are urgently required to develop next-generation antibiotics. We investigated mannitol-1-phosphate dehydrogenase of S. aureus USA300 (SaM1PDH), a key enzyme regulating intracellular...

    Thanh Nguyen, Truc Kim, Hai Minh Ta, Won Sik Yeo, Jongkeun Choi, Pushpak Mizar, Seung Seo Lee, Taeok Bae, Akhilesh Kumar Chaurasia, Kyeong Kyu Kim
  • Open Access
    Structure of <em>Vibrio</em> FliL, a New Stomatin-like Protein That Assists the Bacterial Flagellar Motor Function
    Research Article | Molecular Biology and Physiology
    Structure of Vibrio FliL, a New Stomatin-like Protein That Assists the Bacterial Flagellar Motor Function

    Some flagellated bacteria regulate motor torque in response to the external load change. This behavior is critical for survival, but the mechanism has remained unknown. Here, we focused on a key protein, FliL of Vibrio alginolyticus, and solved the crystal structure of its periplasmic region (FliLPeri). FliLPeri reveals striking structural...

    Norihiro Takekawa, Miyu Isumi, Hiroyuki Terashima, Shiwei Zhu, Yuuki Nishino, Mayuko Sakuma, Seiji Kojima, Michio Homma, Katsumi Imada
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