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Mechanisms by which small molecules of diverse chemotypes arrest Sec14 lipid transfer activity
Chen, X. R., Poudel, L., Hong, Z., Johnen, P., Katti, S., Tripathi, A., … Igumenova, T. I. (2023). Mechanisms by which small molecules of diverse chemotypes arrest Sec14 lipid transfer activity. Journal of Biological Chemistry, 299(2), 102861 (21 pp.). https://doi.org/10.1016/j.jbc.2022.102861
Structures of an unusual 3-hydroxyacyl dehydratase (FabZ) from a ladderane-producing organism with an unexpected substrate preference
Dietl, A., Wellach, K., Mahadevan, P., Mertes, N., Winter, S. L., Kutsch, T., … Barends, T. R. M. (2023). Structures of an unusual 3-hydroxyacyl dehydratase (FabZ) from a ladderane-producing organism with an unexpected substrate preference. Journal of Biological Chemistry, 299(5), 104602 (15 pp.). https://doi.org/10.1016/j.jbc.2023.104602
Structures of calmodulin–melittin complexes show multiple binding modes lacking classical anchoring interactions
Dürvanger, Z., Juhász, T., Liliom, K., & Harmat, V. (2023). Structures of calmodulin–melittin complexes show multiple binding modes lacking classical anchoring interactions. Journal of Biological Chemistry, 299(4), 104596 (15 pp.). https://doi.org/10.1016/j.jbc.2023.104596
Arsenite oxidase in complex with antimonite and arsenite oxyanions: insights into the catalytic mechanism
Engrola, F., Correia, M. A. S., Watson, C., Romão, C. C., Veiros, L. F., Romão, M. J., … Santini, J. M. (2023). Arsenite oxidase in complex with antimonite and arsenite oxyanions: insights into the catalytic mechanism. Journal of Biological Chemistry, 299(8), 105036 (9 pp.). https://doi.org/10.1016/j.jbc.2023.105036
Characterization of a novel cysteine-less Cu/Zn-superoxide dismutase in <em>Paenibacillus lautus</em> missing a conserved disulfide bond
Furukawa, Y., Shintani, A., Narikiyo, S., Sue, K., Akutsu, M., & Muraki, N. (2023). Characterization of a novel cysteine-less Cu/Zn-superoxide dismutase in Paenibacillus lautus missing a conserved disulfide bond. Journal of Biological Chemistry, 299(8), 105040 (13 pp.). https://doi.org/10.1016/j.jbc.2023.105040
Biophysical and structural characterization of the impacts of MET phosphorylation on tepotinib binding
Grädler, U., Schwarz, D., Wegener, A., Eichhorn, T., Bandeiras, T. M., Freitas, M. C., … Bomke, J. (2023). Biophysical and structural characterization of the impacts of MET phosphorylation on tepotinib binding. Journal of Biological Chemistry, 299(11), 105328 (14 pp.). https://doi.org/10.1016/j.jbc.2023.105328
1-deoxy-D-xylulose-5-phosphate synthase from Pseudomonas <em>aeruginosa </em>and <em>Klebsiella pneumoniae</em> reveals conformational changes upon cofactor binding
Hamid, R., Adam, S., Lacour, A., Monjas, L., Köhnke, J., & Hirsch, A. K. H. (2023). 1-deoxy-D-xylulose-5-phosphate synthase from Pseudomonas aeruginosa and Klebsiella pneumoniae reveals conformational changes upon cofactor binding. Journal of Biological Chemistry, 299(9), 105152 (11 pp.). https://doi.org/10.1016/j.jbc.2023.105152
Intrinsic structural vulnerability in the hydrophobic core induces species-specific aggregation of canine SOD1 with degenerative myelopathy–linked E40K mutation
Hashimoto, K., Watanabe, S., Akutsu, M., Muraki, N., Kamishina, H., Furukawa, Y., & Yamanaka, K. (2023). Intrinsic structural vulnerability in the hydrophobic core induces species-specific aggregation of canine SOD1 with degenerative myelopathy–linked E40K mutation. Journal of Biological Chemistry, 299(6), 104798 (12 pp.). https://doi.org/10.1016/j.jbc.2023.104798
Ubiquitin-specific protease 11 structure in complex with an engineered substrate mimetic reveals a molecular feature for deubiquitination selectivity
Maurer, S. K., Mayer, M. P., Ward, S. J., Boudjema, S., Halawa, M., Zhang, J., … Dreveny, I. (2023). Ubiquitin-specific protease 11 structure in complex with an engineered substrate mimetic reveals a molecular feature for deubiquitination selectivity. Journal of Biological Chemistry, 299(11), 105300 (15 pp.). https://doi.org/10.1016/j.jbc.2023.105300
<em>N</em>-acetylmuramic acid recognition by MurK kinase from the MurNAc auxotrophic oral pathogen<em> Tannerella forsythia</em>
Stasiak, A. C., Gogler, K., Borisova, M., Fink, P., Mayer, C., Stehle, T., & Zocher, G. (2023). N-acetylmuramic acid recognition by MurK kinase from the MurNAc auxotrophic oral pathogen Tannerella forsythia. Journal of Biological Chemistry, 299(9), 105076 (13 pp.). https://doi.org/10.1016/j.jbc.2023.105076
The Na<sup>+</sup>,K<sup>+</sup>-ATPase in complex with beryllium fluoride mimics an ATPase phosphorylated state
Fruergaard, M. U., Dach, I., Andersen, J. L., Ozol, M., Shahsavar, A., Quistgaard, E. M., … Nissen, P. (2022). The Na+,K+-ATPase in complex with beryllium fluoride mimics an ATPase phosphorylated state. Journal of Biological Chemistry, 298(9), 102317 (12 pp.). https://doi.org/10.1016/j.jbc.2022.102317
Collagen's primary structure determines collagen:HSP47 complex stoichiometry
Abraham, E. T., Oecal, S., Mörgelin, M., Schmid, P. W. N., Buchner, J., Baumann, U., & Gebauer, J. M. (2021). Collagen's primary structure determines collagen:HSP47 complex stoichiometry. Journal of Biological Chemistry, 297(6), 101169 (13 pp.). https://doi.org/10.1016/j.jbc.2021.101169
Ancestral reconstruction of mammalian FMO1 enables structural determination, revealing unique features that explain its catalytic properties
Bailleul, G., Nicoll, C. R., Mascotti, M. L., Mattevi, A., & Fraaije, M. W. (2021). Ancestral reconstruction of mammalian FMO1 enables structural determination, revealing unique features that explain its catalytic properties. Journal of Biological Chemistry, 296, 100221 (13 pp.). https://doi.org/10.1074/jbc.RA120.016297
Identification of difructose dianhydride I synthase/hydrolase from an oral bacterium establishes a novel glycoside hydrolase family
Kashima, T., Okumura, K., Ishiwata, A., Kaieda, M., Terada, T., Arakawa, T., … Fushinobu, S. (2021). Identification of difructose dianhydride I synthase/hydrolase from an oral bacterium establishes a novel glycoside hydrolase family. Journal of Biological Chemistry, 297(5), 101324 (17 pp.). https://doi.org/10.1016/j.jbc.2021.101324
Fine-tuning spermidine binding modes in the putrescine binding protein PotF
Kröger, P., Shanmugaratnam, S., Scheib, U., & Höcker, B. (2021). Fine-tuning spermidine binding modes in the putrescine binding protein PotF. Journal of Biological Chemistry, 297(6), 101419 (12 pp.). https://doi.org/10.1016/j.jbc.2021.101419
Crystal structure of the catalytic domain of botulinum neurotoxin subtype A3
Leka, O., Wu, Y., Li, X., & Kammerer, R. A. (2021). Crystal structure of the catalytic domain of botulinum neurotoxin subtype A3. Journal of Biological Chemistry, 296, 100684 (8 pp.). https://doi.org/10.1016/j.jbc.2021.100684
An experimental strategy to probe Gq contribution to signal transduction in living cells
Patt, J., Alenfelder, J., Pfeil, E. M., Voss, J. H., Merten, N., Eryilmaz, F., … Kostenis, E. (2021). An experimental strategy to probe Gq contribution to signal transduction in living cells. Journal of Biological Chemistry, 296, 100472 (17 pp.). https://doi.org/10.1016/j.jbc.2021.100472
Structure-function analysis of pectate lyase Pel3 reveals essential facets of protein recognition by the bacterial type 2 secretion system
Pineau, C., Guschinskaya, N., Gonçalves, I. R., Ruaudel, F., Robert, X., Gouet, P., … Shevchik, V. E. (2021). Structure-function analysis of pectate lyase Pel3 reveals essential facets of protein recognition by the bacterial type 2 secretion system. Journal of Biological Chemistry, 296, 100305 (12 pp.). https://doi.org/10.1016/j.jbc.2021.100305
The molecular basis of spectral tuning in blue- and red-shifted flavin-binding fluorescent proteins
Röllen, K., Granzin, J., Remeeva, A., Davari, M. D., Gensch, T., Nazarenko, V. V., … Krauss, U. (2021). The molecular basis of spectral tuning in blue- and red-shifted flavin-binding fluorescent proteins. Journal of Biological Chemistry, 296, 100662 (13 pp.). https://doi.org/10.1016/j.jbc.2021.100662
Crystallographic snapshots of UDP-glucuronic acid 4-epimerase ligand binding, rotation, and reduction
Iacovino, L. G., Savino, S., Borg, A. J. E., Binda, C., Nidetzky, B., & Mattevi, A. (2020). Crystallographic snapshots of UDP-glucuronic acid 4-epimerase ligand binding, rotation, and reduction. Journal of Biological Chemistry, 295(35), 12461-12473. https://doi.org/10.1074/jbc.ra120.014692
 

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