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Purification, crystallization and X-ray crystallographic analysis of feruloyl-CoA hydratase/lyase of Pseudomonas putida KT2440
Purification, crystallization and X-ray crystallographic analysis of feruloyl-CoA hydratase/lyase of Pseudomonas putida KT2440
Jihye Seok;Kyung-Jin Kim
Çѱ¹±¸Á¶»ý¹°ÇÐȸ / Biodesign Á¦10±Ç Á¦1È£ / 2022 / 12-15 (4 pages)
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Feruloyl-CoA hydratase/lyase (FerB) is an enzyme that catalyzes the final step of converting ferulic acid to biovanillin. In this study, we overexpressed FerB from Pseudomonas putida KT2440 (PpFerB) and purified the protein by Ni-NTA affinity and size-exclusion chromatography. The PpFerB protein was crystallized using hanging-drop vapor-diffusion method in the presence of 25% 1,2-propanediol, 0.1 M sodium phosphate dibasic/citric acid pH 4.2, 5% (w/v) PEG 3000, and 10% (v/v) glycerol at 293 K. X-ray diffraction data were collected to a maximum resolution of 1.65 Å. The PpFerB crystals belong to the space group R3 with unit cell parameters a = 87.7 Å, b = 87.7 Å, c = 198.0 Å, ¥á = 90¡Æ, ¥â = 90¡Æ, ¥ã = 120¡Æ. With six molecules of PpFerB per asymmetric unit, the crystal volume per unit of protein mass is 2.37 Å©ø Da-1, corresponding to a solvent content of approximately 48.08%.
Purification, crystallization and X-ray crystallographic analysis of galactose-1-phosphate uridylyltransferase from Debaryomyces hansenii
Purification, crystallization and X-ray crystallographic analysis of galactose-1-phosphate uridylyltransferase from Debaryomyces hansenii
Sang Woon Lee;Hong Ha Vu;Jeong Ho Chang
Çѱ¹±¸Á¶»ý¹°ÇÐȸ / Biodesign Á¦10±Ç Á¦1È£ / 2022 / 8-11 (4 pages)
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Galactose-1-phosphate uridylyltransferase (GALT) is the second enzyme in the Leloir pathway that reversibly converts galactose-1-phosphate to glucose-1-phosphate. GALT deficiency can cause growth defects in both prokaryotes and eukaryotes. Likewise, in humans, damage of this enzyme leads to a toxic syndrome known as galactosemia type I. In this study, to understand structural features and the underlying molecular mechanism of GALT in yeast, the crystal of GALT from Debaryomyces hansenii was determined at a resolution of 2.8 Å. The crystal of D. hansenii (DhGALT) belonged to the space group C2221, with the unit cell parameters a = 88.5 Å, b = 122.3 Å, c = 154.2 Å, ¥á = ¥â = ¥ã = 90¡Æ. Two macromolecules were present in the asymmetric unit of the crystal. Following its structural determination, further study will be done for elucidating the structural features and reaction mechanism in fungal species.
Current understanding of SARS-CoV-2 papain-like protease inhibitors
Current understanding of SARS-CoV-2 papain-like protease inhibitors
Minhyeong Choi;Sangwoo Kang;Ane Martiartu;Donghyuk Shin
Çѱ¹±¸Á¶»ý¹°ÇÐȸ / Biodesign Á¦10±Ç Á¦1È£ / 2022 / 1-7 (7 pages)
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The spread of SARS-CoV-2 has been the cause of the ongoing COVID-19 global pandemic, which has increased morbidity and mortality worldwide. SARS-CoV-2 has two proteases that play an essential role in its spread, promoting replication by cleaving viral polyproteins. One of these two proteases, PLpro suppresses the host immune response through deubiquitination and deISGylation. Since PLpro plays a vital role in viral spread, there is a need for research on therapeutic agents that target it. In this review, we identify and classify several types of PLpro inhibitors.
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Crystallization and preliminary diffraction analysis of the phosphatase domain of PTPN14 in the human papillomavirus E7 binding-defective mutant form
Crystallization and preliminary diffraction analysis of the phosphatase domain of PTPN14 in the human papillomavirus E7 binding-defective mutant form
Dahwan Lim;Chang Hoon Lee;Ho-Chul Shin;Seung Jun Kim;Bonsu Ku
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A tumor suppressor protein PTPN14 interacts with the oncoprotein E7 of human papillomaviruses, leading to its proteasomal degradation. Introduction of F1044S, G1055Q, and E1095A mutations into its phosphatase domain restored the antitumor activity by impairing the interaction with E7, showing the therapeutic potential of this mutant form against human papillomavirus-involved cancers. In this study, the phosphatase domain of PTPN14 containing the three mutations was produced in an Escherichia coli expression system, purified using Ni-NTA affinity and size exclusion chromatographies, and then crystallized. X-ray diffraction data with a maximum resolution of 1.50 Å were successfully collected, and a preliminary diffraction analysis was conducted. Our crystals belonged to the P21 space group with unit cell parameters of a = 43.9 Å, b = 74.3 Å, c = 47.8 Å, and ¥â = 102.0¡Æ. The asymmetric unit contains one protein molecule with a 45% solvent content and a 2.2 Å3/Da Matthews coefficient.
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New record of the little-known genus Otoblastus (Hymenoptera: Ichneumonidae: Tryphoninae) in South Korea
New record of the little-known genus Otoblastus (Hymenoptera: Ichneumonidae: Tryphoninae) in South Korea
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±¹¸³°ø¿ø¿¬±¸¿ø / ±¹¸³°ø¿ø¿¬±¸Áö Á¦12±Ç Á¦2È£ / 2021 / 25-28 (4 pages)
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¹¶Åö¸Ê½Ã¹ú¾Æ°ú(Subfamily Tryphoninae), ¿ÀÅä¹¶Åö¸Ê½Ã¹ú¼Ó(genus Otoblastus)¿¡ ¼ÓÇÏ´Â 1¹Ì±â·ÏÁ¾ Otoblastus maculator (³ë¶õ¾ó±¼¿ÀÅä¹¶Åö¸Ê½Ã¹ú(½ÅĪ))¸¦ º¸°íÇϰíÀÚ ÇÑ´Ù. ¿ÀÅä¹¶Åö¸Ê½Ã¹ú¼ÓÀº Àü¼¼°è 6Á¾¸¸ÀÌ ±â·ÏµÇ¾î ÀÖ´Â ¸Å¿ì ÀÛÀº ±×·ìÀ̸ç, ÀÌ Áß Çѱ¹»ê ¿ÀÅä¹¶Åö¸Ê½Ã¹ú¼ÓÀº O. marginator 1Á¾¸¸ÀÌ º¸°íµÇ¾î ¿Ô´Ù. º» ¿¬±¸¿¡¼­´Â À̹ø ¿¬±¸¸¦ ÅëÇØ È®ÀÎµÈ O. maculatorÀÇ Áø´Ü±âÀç, »çÁø°ú ´õºÒ¾î ±¸ºÏ±¸Áö¿ª¿¡ ºÐÆ÷ÇÏ´Â º» ¼ÓÀÇ 4Á¾¿¡ ´ëÇÑ °Ë»öÇ¥¸¦ Á¦°øÇÑ´Ù.
Crystal structure of the Fab fragment of burosumab, the first-in-class anti-FGF23 medicine for treating X-linked hypophosphatemia and tumor-induced osteomalacia
Crystal structure of the Fab fragment of burosumab, the first-in-class anti-FGF23 medicine for treating X-linked hypophosphatemia and tumor-induced osteomalacia
Ui Beom Park;Hyun Tae Lee;Yujin Kim;Tae Jun Jeong;Nahyun Gu;Yong-Seok Heo
Çѱ¹±¸Á¶»ý¹°ÇÐȸ / Biodesign Á¦9±Ç Á¦4È£ / 2021 / 59-62 (4 pages)
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Burosumab is a first-in-class therapy approved to treat X-linked hypophosphatemia and tumor-induced osteomalacia, a condition associated with excessive fibroblast growth factor 23 (FGF23) production. This antibody drug directly targets the excessive FGF23 in patients and inhibits its regulation of phosphate homeostasis and vitamin D metabolism. Here, the Fab fragment of burosumab was expressed, purified, and crystallized. The crystals belonged to the space group P21, with unit cell parameters a = 49.51, b = 66.22, c = 62.05 Å, and ¥â = 105.99¡Æ. An asymmetric unit of the crystal contains one Fab fragment with a Matthews coefficient of 1.93 Å3 Da-1. The structure was determined at a resolution of 1.45 Å, with Rwork/Rfree = 0.169/0.196. The complementarity determining regions of burosumab construct a negatively charged patch, a putative hot spot for FGF23 binding. This high-resolution structure could be used for predicting the binding mode between burosumab and FGF23.
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Integrated cryoEM imaging center at Seoul National University, Korea
Integrated cryoEM imaging center at Seoul National University, Korea
Miji Jeon;Jun Bae Park;Hansol Lee;Gyuhee Kim;Eung Baek Kim;Mingyu Jung;Soung-Hun Roh
Çѱ¹±¸Á¶»ý¹°ÇÐȸ / Biodesign Á¦9±Ç Á¦4È£ / 2021 / 72-77 (6 pages)
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The Center for Macromolecular and Cell Imaging (CMCI) is a core facility equipped with multiple cryo-capable electron microscopes including a 200 kV Thermofisher Glacios, 200 kV JEOL JEM2100Plus and 120 kV FEI TECNAI with direct electron detector technologies. The center also has auxiliary equipment for optimal specimen preparation, such as for protein purification, tissue culture, grid preparation and vitrification. The center offers to the scientific community the best practice of cutting-edge cryogenic electron microscopy (cryoEM) technology for specimen optimization, high-resolution data collection and structure determination. The center also develops the strategy of an integrated cryoEM imaging platform to visualize molecular architectures from purified proteins to cells.
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