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장용대,최가람,조인성,최상호,하남철 한국구조생물학회 2017 Biodesign Vol.5 No.1
LysR-type transcriptional regulators (LTTRs) belong to the largest family of transcriptional regulators in prokaryotes. However, the crystal structures of only a few full-length LTTRs have been determined. LTTR HypT (also known as YjiE orQseD) from Escherichia coli specifically senses hypochlorite to protect oxidation damage by hypochlorite generated bythe host immune system. In the genome of the highly virulent bacteria, Vibrio vulnificus, VV2_1132 showed the highestsequence similarity to E. coli HypT. In this study, we overexpressed full-length VV2_1132 in an E. coli expression systemand crystallized the protein. The crystal diffracted X-rays to 2.2 Å resolution and belonged to the orthogonal space groupP21212, with unit cell parameters a = 57.8, b = 113.5, and c = 220.7 Å. Cell content analysis predicted that the asymmetricunit may contain four molecules of VV2_1132. For the case of four molecules in the asymmetric unit, the Matthewscoefficient was 2.70 Å3/Da with a solvent content of 54.5%. We are currently identifying the crystal structure of VV2_1132using anomalous signals from selenomethione-substituted crystals. This crystal structure will help elucidate the functionand action mechanism of VV2_1132, which may be involved in the pathogenesis of V. vulnificus.
장용대,박영하,이재우,조인성,박채운,석영재,하남철 한국구조생물학회 2017 Biodesign Vol.5 No.2
Many kinds of nucleotides are differentially synthesized and degraded in response to external and internal signaling inbacterial cells. Cyclic di-GMP (c-di-GMP) is ubiquitous bacterial nucleotide secondary signaling molecule, and is involvedin virulence, antibiotic resistance, biofilm formation and cell division. VCA0593 was predicted or screened as a c-di-GMPor 5’-phosphguanylyl-(3’,5’)-guanosine binding protein in Vibrio cholerae genome by genome-wide system approaches,suggesting that VCA0593 might be involved in a c-di-GMP-mediated signaling pathway. In this study, the full-lengthVCA0593 was overexpressed in the E. coli expression system, and successfully crystallized. X-rays were diffracted by thecrystals to 1.60 Å resolution, revealing that the crystals belong to space group P21212, with unit cell parameters a = 68.9, b= 149.0, and c = 58.9 Å. According to cell content analysis, the asymmetric unit was expected to contain two molecules ofVCA0593. The molecular replacement was not available due to lack of the homologous models. We are now under way tosolve the crystal structure using the anomalous signals from Zn-soaked crystals. The crystal structure would help revealthe function of the protein and its mechanism of action, which could be associated with the pathogenesis of V. cholerae.
장용대,최가람,홍석호,조인성,안진숙,최상호,하남출 한국분자세포생물학회 2018 Molecules and cells Vol.41 No.4
LysR-type transcriptional regulators (LTTRs) contain an N-terminal DNA binding domain (DBD) and a C-terminal regulatory domain (RD). Typically, LTTRs function as homotetramers. VV2_1132 was identified in Vibrio vulnificus as an LTTR that is a homologue of HypT (also known as YjiE or QseD) in Escherichia coli. In this study, we determined the crystal structure of full-length VV2_1132 at a resolution of 2.2 Å, thereby revealing a novel combination of the domains in the tetrameric assembly. Only one DBD dimer in the tetramer can bind to DNA, because the DNA binding motifs of the other DBD dimer are completely buried in the tetrameric assembly. Structural and functional analyses of VV2_1132 suggest that it might not perform the same role as E. coli HypT, indicating that further study is required to elucidate the function of this gene in V. vulnificus. The unique structure of VV2_1132 extends our knowledge of LTTR function and mechanisms of action.