The crystallization of apo-form UMP kinase from Xanthomonas campestris is significantly improved in a strong magnetic field

Jhe Le Tu, Ko Hsin Chin, Andrew H.J. Wang, Shan Ho Chou

研究成果: 雜誌貢獻文章同行評審

5 引文 斯高帕斯(Scopus)

摘要

Bacterial UMP kinases (UMPKs) are crucial enzymes that are responsible for microbial UTP biosynthesis. Interestingly, eukaryotic and prokaryotic cells use different enzymes for UMP-phosphorylation reactions. Prokaryotic UMPKs are thus believed to be potential targets for antimicrobial drug development. Here, the cloning, expression and crystallization of SeMet-substituted XC1936, a bacterial UMPK from Xanthomonas campestris pathovar campestris, are reported. The crystallization of the apo-form UMPK was found to be significantly improved in a strong magnetic field; the crystals diffracted to a resolution of 2.35 Å, a dramatic improvement over the original value of 3.6 Å. Preliminary structural analyses of apo-form XC1936 using crystals grown in a strong magnetic field clearly reveal well defined loop regions involved in substrate-analogue binding that were previously not visible. Crystallization in a strong magnetic field thus was found to be indispensable in determining the flexible region of the XC1936 UMPK structure.

原文英語
文章編號fw5136
頁(從 - 到)438-442
頁數5
期刊Acta Crystallographica Section F: Structural Biology and Crystallization Communications
63
發行號5
DOIs
出版狀態已發佈 - 4月 28 2007
對外發佈

ASJC Scopus subject areas

  • 生物物理學
  • 結構生物學
  • 生物化學
  • 遺傳學
  • 凝聚態物理學

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