Publications by authors named "Bo Gyeong Jeong"

Article Synopsis
  • Researchers created membranes using a combination of porous silicon dioxide (SiO) and poly(vinylidene fluoride) (PVdF) through a process called electrospinning.
  • The composite membranes have tunable thickness and low thermal shrinkage, demonstrating stability at high temperatures but showing changes in electrical properties at around 170°C to 225°C.
  • Even after exposure to temperatures over 270°C, the membranes maintained their structure without collapsing, indicating good thermal resilience.
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Docking domains (DDs) located at the C- and N-termini of polypeptides play a crucial role in directing the assembly of polyketide synthases (PKSs), which are multienzyme complexes. Here, we determined the crystal structure of a complex comprising the C-terminal DD (DD) and N-terminal DD (DD) of macrolactin trans-acyltransferase (AT) PKS that were fused to a functional enzyme, AmpC EC2 β-lactamase. Interface analyses of the DD/DD complex revealed the molecular intricacies in the core section underpinning the precise DD assembly.

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Objectives: Stenotrophomonas spp. intrinsically resistant to many β-lactam antibiotics are found throughout the environment. CESS-1 identified in Stenotrophomonas sp.

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Phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P] is implicated in various processes, including hormone-induced signal transduction, endocytosis, and exocytosis in the plasma membrane. However, how HO accumulation regulates the levels of PtdIns(4,5)P in the plasma membrane in cells stimulated with epidermal growth factors (EGFs) is not known. We show that a plasma membrane PtdIns(4,5)P-degrading enzyme, synaptojanin (Synj) phosphatase, is inactivated through oxidation by HO.

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Fibroblast growth factor 21 (FGF21) has pharmaceutical potential against obesity-related metabolic disorders, including non-alcoholic fatty liver disease. Since thermal stability is a desirable factor for therapeutic proteins, we investigated the thermal behavior of human FGF21. FGF21 remained soluble after heating; thus, we examined its temperature-induced structural changes using circular dichroism (CD).

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Article Synopsis
  • Metallo-β-lactamase (MBL) superfamily proteins share a common structural fold and carry out diverse functions through metal-based catalysis, but most members remain poorly understood.
  • The protein TW9814, a hypothetical member of this superfamily, has been identified as a phosphodiesterase that requires divalent metal ions like manganese(II) or nickel(II) for activity, showcasing its dimeric structure as crucial for function.
  • TW9814 exhibits high catalytic efficiency under alkaline conditions, with its activity being uniquely regulated by a disulfide bond, highlighting its potential as a model for studying other MBL superfamily proteins.
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Article Synopsis
  • AmpC BER is an advanced β-lactamase enzyme with a unique structural modification that enhances its ability to resist antibiotics, specifically owing to a two-amino-acid insertion that broadens its active site.
  • Researchers found that halisulfates, derived from marine sponges, fit well into the active site of AmpC BER and effectively inhibit its activity, with halisulfate 5 showing strong inhibition comparable to a known inhibitor called avibactam.
  • The study suggests that combining β-lactam antibiotics with new inhibitors like halisulfates could be an effective strategy against infections caused by bacteria that produce resistant enzymes, addressing the challenge of emerging antibiotic resistance.
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The hydrolysis of β-lactam antibiotics by class C β-lactamases proceeds through the acylation and the rate-determining deacylation steps mediated by the nucleophilic serine and the deacylation water, respectively. The pose of poor substrates such as carbapenems in the acylated enzyme is responsible for the low efficient deacylation reaction. Here we present the crystal structures of the Y150F variant of the ACC-1 class C β-lactamase in the apo and acylated states.

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β-Lactamase-mediated resistance to β-lactam antibiotics has been significantly threatening the efficacy of these clinically important antibacterial drugs. Although some β-lactamase inhibitors are prescribed in combination with β-lactam antibiotics to overcome this resistance, the emergence of enzymes resistant to current inhibitors necessitates the development of novel β-lactamase inhibitors. In this study, we evaluated the inhibitory effect of dinucleotides on an extended-spectrum class C β-lactamase, AmpC BER.

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