Publications
31 results found
Kotei PA, Paley DW, Oklejas V, et al., 2024, Engineering Supramolecular Hybrid Architectures with Directional Organofluorine Bonds, Small Science, Vol: 4, ISSN: 2688-4046
<jats:p>Understanding how chemical modifications alter the atomic‐scale organization of materials is of fundamental importance in materials engineering and the target of considerable efforts in computational prediction. Incorporating covalent and noncovalent interactions in designing crystals while “piggybacking” on the driving force of molecular self‐assembly has augmented efforts to understand the emergence of complex structures using directed synthesis. In this work, microcrystalline powders of the silver 2‐, 3‐, and 4‐fluorobenzenethiolates are prepared and their structures are resolved by small‐molecule serial femtosecond X‐ray crystallography. These three compounds enable the emergence and role of supramolecular synthons in the crystal structures of 3D metal‐organic chalcogenolates to be examined. The unique divergence in their optoelectronic, morphological, and structural behaviors is assessed. The extent of CHF interactions and their influence on the structure and the observed trends in the thermal stability of the crystals are quantified through theoretical calculations and thermogravimetric analysis.</jats:p>
Stępień P, Świątek S, Robles MYY, et al., 2023, CRAFTing Delivery of Membrane Proteins into Protocells using Nanodiscs., ACS Appl Mater Interfaces, Vol: 15, Pages: 56689-56701
For the successful generative engineering of functional artificial cells, a convenient and controllable means of delivering membrane proteins into membrane lipid bilayers is necessary. Here we report a delivery system that achieves this by employing membrane protein-carrying nanodiscs and the calcium-dependent fusion of phosphatidylserine lipid membranes. We show that lipid nanodiscs can fuse a transported lipid bilayer with the lipid bilayers of small unilamellar vesicles (SUVs) or giant unilamellar vesicles (GUVs) while avoiding recipient vesicles aggregation. This is triggered by a simple, transient increase in calcium concentration, which results in efficient and rapid fusion in a one-pot reaction. Furthermore, nanodiscs can be loaded with membrane proteins that can be delivered into target SUV or GUV membranes in a detergent-independent fashion while retaining their functionality. Nanodiscs have a proven ability to carry a wide range of membrane proteins, control their oligomeric state, and are highly adaptable. Given this, our approach may be the basis for the development of useful tools that will allow bespoke delivery of membrane proteins to protocells, equipping them with the cell-like ability to exchange material across outer/subcellular membranes.
Travin DYY, Jouan R, Vigouroux A, et al., 2023, Dual-Uptake Mode of the Antibiotic Phazolicin Prevents Resistance Acquisition by Gram-Negative Bacteria, MBIO, ISSN: 2150-7511
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- Citations: 1
Travin DY, Vigouroux A, Inaba-Inoue S, et al., 2022, The antibiotic phazolicin displays a dual mode of uptake in Gram-negative bacteria
<jats:title>ABSTRACT</jats:title><jats:p>Phazolicin (PHZ) is a peptide antibiotic exhibiting narrow-spectrum activity against rhizobia closely related to its producer <jats:italic>Rhizobium</jats:italic> sp. Pop5. Using genetic and biochemical techniques, we here identified BacA and YejABEF as two importers of PHZ in a sensitive model strain <jats:italic>Sinorhizobium meliloti</jats:italic> Sm1021. BacA and YejABEF are members of SLiPT and ABC transporter families of non-specific peptide importers, respectively. The uptake of PHZ by two distinct families of transporters dramatically decreases the naturally occurring rate of resistance. Moreover, since both BacA and YejABEF are essential for the development of functional symbiosis of rhizobia with leguminous plants, the acquisition of PHZ resistance via the inactivation of transporters is further disfavoured since single <jats:italic>bacA</jats:italic> or <jats:italic>yejABEF</jats:italic> mutants are unable to propagate in root nodules. Crystal structures of the periplasmic subunit YejA from <jats:italic>S. meliloti</jats:italic> and <jats:italic>Escherichia coli</jats:italic> revealed fortuitous bound peptides, suggesting a non-specific peptide-binding mechanism that facilitates the uptake of PHZ and other antimicrobial peptides.</jats:p><jats:sec><jats:title>SIGNIFICANCE</jats:title><jats:p>Many bacteria produce antimicrobial peptides to eliminate competitors and create an exclusive niche. These peptides kill bacteria by either membrane disruption or inhibiting essential intracellular processes. The Achilles heel of the latter type of antimicrobials is their dependence on transporters to enter the susceptible bacteria since mutations in such transporters result in resistance. We describe here how the ribosome-targeting peptide phazolicin, produced by <jats:italic>Rhizobium</jats:italic&g
Ghilarov D, Inaba-Inoue S, Stepien P, et al., 2021, Molecular mechanism of SbmA, a promiscuous transporter exploited by antimicrobial peptides, Science Advances, Vol: 7, Pages: 1-10, ISSN: 2375-2548
Antibiotic metabolites and antimicrobial peptides mediate competition between bacterial species. Many of them hijack inner and outer membrane proteins to enter cells. Sensitivity of enteric bacteria to multiple peptide antibiotics is controlled by the single inner membrane protein SbmA. To establish the molecular mechanism of peptide transport by SbmA and related BacA, we determined their cryo–electron microscopy structures at 3.2 and 6 Å local resolution, respectively. The structures show a previously unknown fold, defining a new class of secondary transporters named SbmA-like peptide transporters. The core domain includes conserved glutamates, which provide a pathway for proton translocation, powering transport. The structures show an outward-open conformation with a large cavity that can accommodate diverse substrates. We propose a molecular mechanism for antibacterial peptide uptake paving the way for creation of narrow-targeted therapeutics.
Inaba S, Shiota A, Yoshida T, et al., 2019, Site-specific observation of the conformational change of a protein with <SUP>15</SUP>N-labeled Tyr residues using NMR, ANALYTICAL BIOCHEMISTRY, Vol: 574, Pages: 34-38, ISSN: 0003-2697
Oda M, Xi Z, Inaba S, et al., 2019, Binding thermodynamics of metal ions to HIV-1 ribonuclease H domain, JOURNAL OF THERMAL ANALYSIS AND CALORIMETRY, Vol: 135, Pages: 2647-2653, ISSN: 1388-6150
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- Citations: 6
Inaba S, Kamiya N, Bekker G-J, et al., 2019, Folding thermodynamics of PET-hydrolyzing enzyme Cut190 depending on Ca<SUP>2+</SUP> concentration, JOURNAL OF THERMAL ANALYSIS AND CALORIMETRY, Vol: 135, Pages: 2655-2663, ISSN: 1388-6150
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- Citations: 23
Inaba-Inoue S, Inoue K, Hikima T, et al., 2019, CRYSTAL AND SOLUTION STRUCTURES OF SH2 DOMAIN OF SIGNALING MOLECULE IN COMPLEX WITH THE CO-STIMULATORY RECEPTOR CD28, ACTA CRYSTALLOGRAPHICA A-FOUNDATION AND ADVANCES, Vol: 75, Pages: E69-E69, ISSN: 2053-2733
Hosoe Y, Numoto N, Inaba S, et al., 2019, Structural and functional properties of Grb2 SH2 dimer in CD28 binding, BIOPHYSICS AND PHYSICOBIOLOGY, Vol: 16, Pages: 80-88
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- Citations: 9
Oda M, Yamagami Y, Inaba S, et al., 2018, Enzymatic hydrolysis of PET: functional roles of three Ca<SUP>2+</SUP> ions bound to a cutinase-like enzyme, Cut190*, and its engineering for improved activity, APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, Vol: 102, Pages: 10067-10077, ISSN: 0175-7598
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- Citations: 61
Numoto N, Kamiya N, Bekker G-J, et al., 2018, Structural Dynamics of the PET-Degrading Cutinase-like Enzyme from <i>Saccharomonospora viridis</i> AHK190 in Substrate-Bound States Elucidates the Ca<SUP>2+</SUP>-Driven Catalytic Cycle, BIOCHEMISTRY, Vol: 57, Pages: 5289-5300, ISSN: 0006-2960
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- Citations: 43
Hosoe Y, Inaba S, Sekiguchi H, et al., 2018, DNA-binding induced conformational change of c-Myb R2R3 analyzed using diffracted X-ray tracking, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Vol: 503, Pages: 338-343, ISSN: 0006-291X
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- Citations: 4
Oda M, Inaba S, Kamiya N, et al., 2018, Structural and thermodynamic characterization of endo-1,3-β-glucanase: Insights into the substrate recognition mechanism, BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, Vol: 1866, Pages: 415-425, ISSN: 1570-9639
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- Citations: 14
Inaba S, Fukada H, Oda M, 2018, Effect of a salt-bridge between inter-repeats on the 3D structure of the c-Myb DNA-binding domain revealed by thermodynamic analysis, JOURNAL OF THERMAL ANALYSIS AND CALORIMETRY, Vol: 131, Pages: 335-341, ISSN: 1388-6150
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- Citations: 8
Shiota A, Inaba S, Oda M, 2018, Effects of active site residues of 3-hydroxysteroid dehydrogenase from <i>pseudomonas</i> sp b-0831 on its catalysis and cofactor binding, BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, Vol: 82, Pages: 1702-1707, ISSN: 0916-8451
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- Citations: 2
Usui D, Inaba S, Kamatari YO, et al., 2017, Light-chain residue 95 is critical for antigen binding and multispecificity of monoclonal antibody G2, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Vol: 490, Pages: 1205-1209, ISSN: 0006-291X
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- Citations: 4
Usui D, Inaba S, Sekiguchi H, et al., 2017, First observation of metal ion-induced structural fluctuations of α-helical peptides by using diffracted X-ray tracking, BIOPHYSICAL CHEMISTRY, Vol: 228, Pages: 81-86, ISSN: 0301-4622
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- Citations: 5
Miki A, Inaba S, Maruno T, et al., 2017, Tryptophan introduction can change -glucan binding ability of the carbohydrate-binding module of endo-1,3--glucanase, BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, Vol: 81, Pages: 951-957, ISSN: 0916-8451
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- Citations: 3
Sato Y, Inaba S, Fukada H, et al., 2017, Pronounced effect of hapten binding on thermal stability of an anti-(4-hydroxy-3-nitrophenyl)acetyl antibody possessing a glycine residue at position 95 of the heavy chain, MOLECULAR IMMUNOLOGY, Vol: 85, Pages: 130-136, ISSN: 0161-5890
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- Citations: 3
Inaba S, Numoto N, Ogawa S, et al., 2017, Crystal Structures and Thermodynamic Analysis Reveal Distinct Mechanisms of CD28 Phosphopeptide Binding to the Src Homology 2 (SH2) Domains of Three Adaptor Proteins, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 292, Pages: 1052-1060
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- Citations: 15
INABA S, 2017, Structural and Functional Analysis of DNA-binding Protein under Physiological Conditions, Seibutsu Butsuri, Vol: 57, Pages: 257-258, ISSN: 0582-4052
Sato Y, Tanaka Y, Inaba S, et al., 2016, Structural dynamics of a single-chain Fv antibody against (4-hydroxy-3-nitrophenyl)acetyl, INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, Vol: 91, Pages: 151-157, ISSN: 0141-8130
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- Citations: 13
Oda M, Tanabe Y, Noda M, et al., 2016, Structural and binding properties of laminarin revealed by analytical ultracentrifugation and calorimetric analyses, CARBOHYDRATE RESEARCH, Vol: 431, Pages: 33-38, ISSN: 0008-6215
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- Citations: 9
Inaba S, Fukada H, Oda M, 2016, Thermodynamic effects of a linker region between two repeats of a protein, c-Myb R2R3, on its stability and structural dynamics, JOURNAL OF THERMAL ANALYSIS AND CALORIMETRY, Vol: 123, Pages: 1763-1767, ISSN: 1388-6150
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- Citations: 4
Inaba S, Fukada H, Oda M, 2016, Folding thermodynamics of c-Myb DNA-binding domain in correlation with its α-helical contents, INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, Vol: 82, Pages: 725-732, ISSN: 0141-8130
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- Citations: 6
Inaba S, Maeno A, Sakurai K, et al., 2015, Functional conformer of c-Myb DNA-binding domain revealed by variable temperature studies, FEBS JOURNAL, Vol: 282, Pages: 4497-4514, ISSN: 1742-464X
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- Citations: 7
Miki A, Inaba S, Baba T, et al., 2015, Structural and physical properties of collagen extracted from moon jellyfish under neutral pH conditions, BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY, Vol: 79, Pages: 1603-1607, ISSN: 0916-8451
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- Citations: 13
Inaba S, Fukada H, Ikegami T, et al., 2013, Thermodynamic effects of multiple protein conformations on stability and DNA binding, ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, Vol: 537, Pages: 225-232, ISSN: 0003-9861
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- Citations: 27
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