Skip Navigation
Skip to contents

Journal of Microbiology : Journal of Microbiology

OPEN ACCESS
SEARCH
Search

Author index

Page Path
HOME > Browse Articles > Author index
Search
Jin Myung Choi 2 Articles
The crystal structure of methanol dehydrogenase, a quinoprotein from the marine methylotrophic bacterium Methylophaga aminisulfidivorans MPT
Thinh-Phat Cao , Jin Myung Choi , Si Wouk Kim , Sung Haeng Lee
J. Microbiol. 2018;56(4):246-254.   Published online February 28, 2018
DOI: https://doi.org/10.1007/s12275-018-7483-y
  • 938 View
  • 0 Download
  • 18 Crossref
AbstractAbstract PDF
The first crystal structure of a pyrroloquinoline quinone (PQQ)-dependent methanol dehydrogenase (MDH) from a marine methylotrophic bacterium, Methylophaga aminisulfidivorans MPT (MDHMas), was determined at 1.7 Å resolution. The active form of MDHMas (or MDHIMas) is a heterotetrameric α2β2, where each β-subunit assembles on one side of each of the α-subunits, in a symmetrical fashion, so that two β-subunits surround the two PQQ-binding pockets on the α-subunits. The active site consists of a PQQ molecule surrounded by a β-propeller fold for each α-subunit. Interestingly, the PQQ molecules are coordinated by a Mg2+ ion, instead of the Ca2+ ion that is commonly found in the terrestrial MDHI, indicating the efficiency of osmotic balance regulation in the high salt environment. The overall interaction of the β-subunits with the α-subunits appears tighter than that of terrestrial homologues, suggesting the efficient maintenance of MDHIMas integrity in the sea water environment to provide a firm basis for complex formation with MxaJMas or Cyt cL. With the help of the features mentioned above, our research may enable the elucidation of the full molecular mechanism of methanol oxidation by taking advantage of marine bacterium-originated proteins in the methanol oxidizing system (mox), including MxaJ, as the attainment of these proteins from terrestrial bacteria for structural studies has not been successful.

Citations

Citations to this article as recorded by  
  • A PQQ-dependent oxidoreductase in Trypanosoma cruzi reveals a novel redox activity in a eukaryotic pathogen
    Juan Pablo Gallardo, Walter Jesús Lapadula, Micaela Soledad Ossowski, Gabriela Teresa Niemirowicz, Maximiliano Juri Ayub, Karina Andrea Gómez, Mariana Potenza
    Frontiers in Cellular and Infection Microbiology.2026;[Epub]     CrossRef
  • Dynamic properties of confined water inside hydrophilic surfaces
    One-Sun Lee, Sung Haeng Lee
    Chemistry Letters.2025;[Epub]     CrossRef
  • Breeding and genomic analysis of the high PQQ-producing strain Hyphomicrobium denitrificans NJTU3-43
    Jingxiang Sun, Hongting Yue, Weixiu Ma, Shuwen Ding, Yujia Jiang, Wenming Zhang, Wankui Jiang, Fengxue Xin, Min Jiang
    Chemical Engineering Journal.2025; 511: 162001.     CrossRef
  • Mechanistic Interrogation of a PQQ and Rare Earth-Dependent Artificial Metalloenzyme
    Mohd Taher, Peter J. Thompson, Carlos Nava-Matadamas, Austin T. Bruchs, Jennifer Bridwell-Rabb, Lisa Olshansky
    Journal of the American Chemical Society.2025; 147(41): 37104.     CrossRef
  • Antibacterial mechanisms of lipid extraction by MXene nanosheets
    One-Sun Lee, Sung Haeng Lee
    Chemistry Letters.2025;[Epub]     CrossRef
  • Computational insights into the molecular dynamics of the binding of ligands in the methanol dehydrogenase
    One-Sun Lee, Sung Haeng Lee
    Chemistry Letters.2024;[Epub]     CrossRef
  • Formaldehyde: An Essential Intermediate for C1 Metabolism and Bioconversion
    Mengshi Jia, Mengge Liu, Jiawen Li, Wankui Jiang, Fengxue Xin, Wenming Zhang, Yujia Jiang, Min Jiang
    ACS Synthetic Biology.2024; 13(11): 3507.     CrossRef
  • Unveiling the Secrets of Calcium-Dependent Proteins in Plant Growth-Promoting Rhizobacteria: An Abundance of Discoveries Awaits
    Betina Cecilia Agaras, Cecilia Eugenia María Grossi, Rita María Ulloa
    Plants.2023; 12(19): 3398.     CrossRef
  • The biochemistry of lanthanide acquisition, trafficking, and utilization
    Emily R. Featherston, Joseph A. Cotruvo
    Biochimica et Biophysica Acta (BBA) - Molecular Cell Research.2021; 1868(1): 118864.     CrossRef
  • Bioinorganic insights of the PQQ-dependent alcohol dehydrogenases
    Pedro D. Sarmiento-Pavía, Martha E. Sosa-Torres
    JBIC Journal of Biological Inorganic Chemistry.2021; 26(2-3): 177.     CrossRef
  • Bioinformatic analysis of subfamily-specific regions in 3D-structures of homologs to study functional diversity and conformational plasticity in protein superfamilies
    Daria Timonina, Yana Sharapova, Vytas Švedas, Dmitry Suplatov
    Computational and Structural Biotechnology Journal.2021; 19: 1302.     CrossRef
  • Methanol Dehydrogenases as a Key Biocatalysts for Synthetic Methylotrophy
    Thien-Kim Le, Yu-Jin Lee, Gui Hwan Han, Soo-Jin Yeom
    Frontiers in Bioengineering and Biotechnology.2021;[Epub]     CrossRef
  • Lanthanide-dependent alcohol dehydrogenases require an essential aspartate residue for metal coordination and enzymatic function
    Nathan M. Good, Matthias Fellner, Kemal Demirer, Jian Hu, Robert P. Hausinger, N. Cecilia Martinez-Gomez
    Journal of Biological Chemistry.2020; 295(24): 8272.     CrossRef
  • Zebra2: advanced and easy-to-use web-server for bioinformatic analysis of subfamily-specific and conserved positions in diverse protein superfamilies
    Dmitry Suplatov, Yana Sharapova, Elizaveta Geraseva, Vytas Švedas
    Nucleic Acids Research.2020; 48(W1): W65.     CrossRef
  • Biological Pincer Complexes
    Jorge L. Nevarez, Aiko Turmo, Jian Hu, Robert P. Hausinger
    ChemCatChem.2020; 12(17): 4242.     CrossRef
  • Crystal structure of Cytochrome cL from the aquatic methylotrophic bacterium Methylophaga aminisulfidivorans MPT
    Suparna Ghosh, Immanuel Dhanasingh, Jaewon Ryu, Si Wouk Kim, Sung Haeng Lee
    Journal of Microbiology and Biotechnology.2020; 30(8): 1261.     CrossRef
  • New metal cofactors and recent metallocofactor insights
    Robert P Hausinger
    Current Opinion in Structural Biology.2019; 59: 1.     CrossRef
  • Lanthanides‐based catalysis in eukaryotes
    Giovanna De Simone, Fabio Polticelli, Silvio Aime, Paolo Ascenzi
    IUBMB Life.2018; 70(11): 1067.     CrossRef
Structural insight for substrate tolerance to 2-deoxyribose-5-phosphate aldolase from the pathogen Streptococcus suis
Thinh-Phat Cao , Joong-Su Kim , Mi-Hee Woo , Jin Myung Choi , Youngsoo Jun , Kun Ho Lee , Sung Haeng Lee
J. Microbiol. 2016;54(4):311-321.   Published online April 1, 2016
DOI: https://doi.org/10.1007/s12275-016-6029-4
  • 948 View
  • 0 Download
  • 6 Crossref
AbstractAbstract PDF
2-deoxyribose-5-phosphate aldolase (DERA) is a class I aldolase that catalyzes aldol condensation of two aldehydes in the active site, which is particularly germane in drug manufacture. Structural and biochemical studies have shown that the active site of DERA is typically loosely packed and displays broader substrate specificity despite sharing conserved folding architecture with other aldolases. The most distinctive structural feature of DERA compared to other aldolases is short and flexible C-terminal region. This region is also responsible for substrate recognition. Therefore, substrate tolerance may be related to the C-terminal structural features of DERA. Here, we determined the crystal structures of full length and C-terminal truncated DERA from Streptococcus suis (SsDERA). In common, both contained the typical (α/β)8 TIM-barrel fold of class I aldolases. Surprisingly, C-terminal truncation
result
ing in missing the last α9 and β8 secondary elements, allowed DERA to maintain activity comparable to the fulllength enzyme. Specifically, Arg186 and Ser205 residues at the C-terminus appeared mutually supplemental or less indispensible for substrate phosphate moiety recognition. Our results suggest that DERA might adopt a shorter C-terminal region than conventional aldolases during evolution pathway, resulting in a broader range of substrate tolerance through active site flexibility.

Citations

Citations to this article as recorded by  
  • An aldolase-dependent phloroglucinol degradation pathway in Collinsella sp. zg1085
    Yating Li, Tong Xu, Yanqin Tu, Tong Li, Yifeng Wei, Yan Zhou, Ning-Yi Zhou
    Applied and Environmental Microbiology.2024;[Epub]     CrossRef
  • Synthetic Activity of Recombinant Whole Cell Biocatalysts Containing 2‐Deoxy‐D‐ribose‐5‐phosphate Aldolase from Pectobacterium atrosepticum
    Romina Fernández Varela, Ana Laura Valino, Eman Abdelraheem, Rosario Médici, Melisa Sayé, Claudio A. Pereira, Peter‐Leon Hagedoorn, Ulf Hanefeld, Adolfo Iribarren, Elizabeth Lewkowicz
    ChemBioChem.2022;[Epub]     CrossRef
  • Rational engineering of 2-deoxyribose-5-phosphate aldolases for the biosynthesis of (R)-1,3-butanediol
    Taeho Kim, Peter J. Stogios, Anna N. Khusnutdinova, Kayla Nemr, Tatiana Skarina, Robert Flick, Jeong Chan Joo, Radhakrishnan Mahadevan, Alexei Savchenko, Alexander F. Yakunin
    Journal of Biological Chemistry.2020; 295(2): 597.     CrossRef
  • Sensitization of colorectal cancer to irinotecan therapy by PARP inhibitor rucaparib
    Titto Augustine, Radhashree Maitra, Jinghang Zhang, Jay Nayak, Sanjay Goel
    Investigational New Drugs.2019; 37(5): 948.     CrossRef
  • Conformational Sampling of the Intrinsically Disordered C-Terminal Tail of DERA Is Important for Enzyme Catalysis
    Marianne Schulte, Dušan Petrović, Philipp Neudecker, Rudolf Hartmann, Jörg Pietruszka, Sabine Willbold, Dieter Willbold, Vineet Panwalkar
    ACS Catalysis.2018; 8(5): 3971.     CrossRef
  • 1H, 13C, and 15N backbone and sidechain resonance assignments of a monomeric variant of E. coli deoxyribose-5-phosphate aldolase
    Marianne Schulte, Matthias Stoldt, Philipp Neudecker, Jӧrg Pietruszka, Dieter Willbold, Vineet Panwalkar
    Biomolecular NMR Assignments.2017; 11(2): 197.     CrossRef

Journal of Microbiology : Journal of Microbiology
TOP