Structure—activity relationship of a recombinant hybrid Manganese superoxide dismutase of Staphylococcus saprophyticus / S. equorum

Retnoningrum, Debbie Soefie; Arumsari, Sekar; Artarini, Anita; Ismaya, Wangsa T.

doi:10.1016/j.ijbiomac.2017.01.096

Cited by 6 publications

(2 citation statements)

References 22 publications

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“…The structure of S. equorum MnSOD ) is dimeric, in which the dimer dissociates at 52-56 °C while the monomer is denatured at 63-68 °C (Retnoningrum et al 2016). S. equorum is a mesophilic bacterium (Indrayati et al The enzyme maintains its activity and dimeric form at either 37 °C and 52°C, but its activity drops significantly with the loss of dimeric form, which undergoes a transition of a native-like structure at ~57 °C (Retnoningrum et al 2017). Alteration of the monomer by an L169W substitution also resulted in a native-like structure that retains the enzyme activity but easily lost the dimeric form .…”

Section: U N C O R R E C T E D G a L L E Y P R O O Fmentioning

confidence: 99%

Relationship and structural diversity of bacterial manganese superoxide dismutases and the strategy for its application in therapy and cosmetics

Retnoningrum

Artarini

Ismaya³

et al. 2022

Microbiol indones

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Manganese superoxide dismutase (MnSOD) from bacteria shares high amino acid sequence homology and nearly identical structure. Despite of that, their characteristics are diverse, which likely due to their bacterial origin and adaptation to the environment. Most importantly, their structural similarity extends to eukaryotic MnSOD, i.e. human. Therefore, structural study of bacterial MnSOD is relevant to its human SOD and henceforth for its use in human as a therapeutic agent or a cosmetic ingredient. Further, eukaryotic MnSOD occurs as a tetramer while almost all of the prokaryotic are dimeric. In this review, relationship between the amino acid sequences and structures of MnSOD as well as their origin and evolution is discussed. The structures of FeSOD and cambialistic SOD, which are MnSOD closest homologs, are visited as the comparison. This study provides an insight to potential safe application of bacterial MnSOD, including necessary modifications to obtain desired characteristics for applications in human.

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Section: U N C O R R E C T E D G a L L E Y P R O O Fmentioning

confidence: 99%

Relationship and structural diversity of bacterial manganese superoxide dismutases and the strategy for its application in therapy and cosmetics

Retnoningrum

Artarini

Ismaya³

et al. 2022

Microbiol indones

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“…equorum MnSOD was overproduced in E. coli BL21 (DE3) cells as a recombinant protein containing a C-terminal His 6 tag. It was subsequently purified according to a previous report (Retnoningrum et al, 2017) with minor modifications, i.e. the buffer used was Tris-buffered saline (TBS; 137 mM NaCl, 2.7 mM KCl, 50 mM Tris-HCl pH 7.5).…”

Section: Preparation Of Recombinant S Equorum Mnsodmentioning

confidence: 99%

The first crystal structure of manganese superoxide dismutase from the genusStaphylococcus

Retnoningrum¹,

Yoshida²,

Arumsari³

et al. 2018

Acta Cryst Sect F

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A recombinant Staphylococcus equorum manganese superoxide dismutase (MnSOD) with an Asp13Arg substitution displays activity over a wide range of pH, at high temperature and in the presence of chaotropic agents, and retains 50% of its activity after irradiation with UVC for up to 45 min. Interestingly, Bacillus subtilis MnSOD does not have the same stability, despite having a closely similar primary structure and thus presumably also tertiary structure. Here, the crystal structure of S. equorum MnSOD at 1.4 Å resolution is reported that may explain these differences. The crystal belonged to space group P321, with unit-cell parameters a = 57.36, b = 57.36, c = 105.76 Å, and contained one molecule in the asymmetric unit. The symmetry operation indicates that the enzyme has a dimeric structure, as found in nature and in B. subtilis MnSOD. As expected, their overall structures are nearly identical. However, the loop connecting the helical and α/β domains of S. equorum MnSOD is shorter than that in B. subtilis MnSOD, and adopts a conformation that allows more direct water-mediated hydrogen-bond interactions between the amino-acid side chains of the first and last α-helices in the latter domain. Furthermore, S. equorum MnSOD has a slightly larger buried area compared with the dimer surface area than that in B. subtilis MnSOD, while the residues that form the interaction in the dimer-interface region are highly conserved. Thus, the stability of S. equorum MnSOD may not originate from the dimeric form alone. Furthermore, an additional water molecule was found in the active site. This allows an alternative geometry for the coordination of the Mn atom in the active site of the apo form. This is the first structure of MnSOD from the genus Staphylococcus and may provide a template for the structural study of other MnSODs from this genus.

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Introducing Intermolecular Interaction to Strengthen the Stability of MnSOD Dimer

Retnoningrum

Yoshida

Pajatiwi

et al. 2023

Appl Biochem Biotechnol

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Structure—activity relationship of a recombinant hybrid Manganese superoxide dismutase of Staphylococcus saprophyticus / S. equorum

Cited by 6 publications

References 22 publications

Relationship and structural diversity of bacterial manganese superoxide dismutases and the strategy for its application in therapy and cosmetics

Relationship and structural diversity of bacterial manganese superoxide dismutases and the strategy for its application in therapy and cosmetics

The first crystal structure of manganese superoxide dismutase from the genusStaphylococcus

Introducing Intermolecular Interaction to Strengthen the Stability of MnSOD Dimer

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