2014
DOI: 10.1107/s2053230x14011005
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Structure ofD-tagatose 3-epimerase-like protein fromMethanocaldococcus jannaschii

Abstract: PDB reference: D-tagatose 3-epimerase-like protein, 3wqoThe crystal structure of a d-tagatose 3-epimerase-like protein (MJ1311p) encoded by a hypothetical open reading frame, MJ1311, in the genome of the hyperthermophilic archaeon Methanocaldococcus jannaschii was determined at a resolution of 2.64 Å . The asymmetric unit contained two homologous subunits, and the dimer was generated by twofold symmetry. The overall fold of the subunit proved to be similar to those of the d-tagatose 3-epimerase from Pseudomona… Show more

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Cited by 3 publications
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“…Through mutation experiments deleting some C-terminal residues, it was found that the existence of a long C-terminal tail was integrant for the dramaticlly thermostability of M. loti LREase (Uechi, Sakuraba, et al, 2013). Interestingly, two D-tagatose 3-epimerase-related proteins from Thermotoga maritima and Methanocaldococcus jannaschii were already determined (Sakuraba, Yoneda, Satomura, Kawakami, & Ohshima, 2009;Uechi, Takata, Yoneda, Ohshima, & Sakuraba, 2014). The main-chain coordinates of the subunit from both of the D-tagatose 3-epimerase-like proteins were found to be similar to those of the ketose 3-epimerases.…”
Section: Overall Structuresmentioning
confidence: 91%
“…Through mutation experiments deleting some C-terminal residues, it was found that the existence of a long C-terminal tail was integrant for the dramaticlly thermostability of M. loti LREase (Uechi, Sakuraba, et al, 2013). Interestingly, two D-tagatose 3-epimerase-related proteins from Thermotoga maritima and Methanocaldococcus jannaschii were already determined (Sakuraba, Yoneda, Satomura, Kawakami, & Ohshima, 2009;Uechi, Takata, Yoneda, Ohshima, & Sakuraba, 2014). The main-chain coordinates of the subunit from both of the D-tagatose 3-epimerase-like proteins were found to be similar to those of the ketose 3-epimerases.…”
Section: Overall Structuresmentioning
confidence: 91%