Draft Genome Sequence of
            <i>Microbacterium</i>
            sp. Strain HM58-2, Which Hydrolyzes Acylhydrazides

Akiyama, Takumi; Ishige, Taichiro; Kanesaki, Yu; Ito, Shinsaku; Oinuma, Ken-Ichi; Takaya, Naoki; Sasaki, Yasuyuki; Yajima, Seishi

doi:10.1128/genomea.00554-16

Cited by 4 publications

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“…In the course of the elucidation of the hydrazide metabolic pathway in Microbacterium sp. HM58-2, the whole genome sequence of the bacterium was obtained, and it was revealed that the hydrazidase gene is located in an operon with an IclR-type transcription factor, which is expected to control the gene expression of the operon (Akiyama et al, 2016).…”

Section: Introductionmentioning

confidence: 99%

Crystal structure of an IclR homologue fromMicrobacteriumsp. strain HM58-2

Akiyama

Yamada

Takaya

et al. 2017

Acta Crystallogr F Struct Biol Commun

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The bacterial transcription factor IclR (isocitrate lyase regulator) is a member of a one-component signal transduction system, which shares the common motif of a helix-turn-helix (HTH)-type DNA-binding domain (DBD) connected to a substrate-binding domain (SBD). Here, the crystal structure of an IclR homologue (Mi-IclR) from Microbacterium sp. strain HM58-2, which catabolizes acylhydrazide as the sole carbon source, is reported. Mi-IclR is expected to regulate an operon responsible for acylhydrazide degradation as an initial step. Native single-wavelength anomalous diffraction (SAD) experiments were performed in combination with molecular replacement. CRANK2 from the CCP4 suite successfully phased and modelled the complete structure of a homotetramer composed of 1000 residues in an asymmetric unit, and the model was refined to 2.1 Å resolution. The overall structure of Mi-IclR shared the same domain combination as other known IclR structures, but the relative geometry between the DBD and SBD differs. Accordingly, the geometry of the Mi-IclR tetramer was unique: the putative substrate-binding site in each subunit is accessible from the outside of the tetramer, as opposed to buried inside as in the previously known IclR structures. These differences in the domain geometry may contribute to the transcriptional regulation of IclRs.

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Section: Introductionmentioning

confidence: 99%