4E22

Structure of cytidine monophosphate kinase from Yersinia pseudotuberculosis

4E22 の概要

• エントリーDOI: 10.2210/pdb4e22/pdb
• 分子名称: Cytidylate kinase, SULFATE ION (3 entities in total)
• 機能のキーワード: p-loop, cmp/atp binding, transferase
• 由来する生物種: Yersinia pseudotuberculosis
• 細胞内の位置: Cytoplasm (By similarity): B1JRD8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27877.74

構造登録者

Clark, E.A.,Acharya, K.R. (登録日: 2012-03-07, 公開日: 2012-12-19, 最終更新日: 2024-02-28)

主引用文献

Walker, N.J.,Clark, E.A.,Ford, D.C.,Bullifent, H.L.,McAlister, E.V.,Duffield, M.L.,Acharya, K.R.,Oyston, P.C.
Structure and function of cytidine monophosphate kinase from Yersinia pseudotuberculosis, essential for virulence but not for survival.
Open Biol, 2:120142-120142, 2012

PubMed Abstract: The need for new antibiotics has become pressing in light of the emergence of antibiotic-resistant strains of human pathogens. Yersinia pestis, the causative agent of plague, is a public health threat and also an agent of concern in biodefence. It is a recently emerged clonal derivative of the enteric pathogen Yersinia pseudotuberculosis. Previously, we developed a bioinformatic approach to identify proteins that may be suitable targets for antimicrobial therapy and in particular for the treatment of plague. One such target was cytidine monophosphate (CMP) kinase, which is an essential gene in some organisms. Previously, we had thought CMP kinase was essential for Y. pseudotuberculosis, but by modification of the mutagenesis approach, we report here the production and characterization of a Δcmk mutant. The isogenic mutant had a growth defect relative to the parental strain, and was highly attenuated in mice. We have also elucidated the structure of the CMP kinase to 2.32 Å, and identified three key residues in the active site that are essential for activity of the enzyme. These findings will have implications for the development of novel CMP kinase inhibitors for therapeutic use.

PubMed: 23271832
DOI: 10.1098/rsob.120142

実験手法

X-RAY DIFFRACTION (2.323 Å)