Crystal structures of putative phosphoglycerate kinases from B. anthracis and C. jejuni

Heping Zheng, Ekaterina V. Filippova, Karolina L. Tkaczuk, Piotr Dworzynski, Maksymilian Chruszcz, Przemyslaw J. Porebski, Zdzislaw Wawrzak, Olena Onopriyenko, Marina Kudritska, Sarah Grimshaw, Alexei Savchenko, Wayne F. Anderson, Wladek Minor

Research output: Contribution to journalArticlepeer-review

7 Scopus citations


Phosphoglycerate kinase (PGK) is indispensable during glycolysis for anaerobic glucose degradation and energy generation. Here we present comprehensive structure analysis of two putative PGKs from Bacillus anthracis str. Sterne and Campylobacter jejuni in the context of their structural homologs. They are the first PGKs from pathogenic bacteria reported in the Protein Data Bank. The crystal structure of PGK from Bacillus anthracis str. Sterne (BaPGK) has been determined at 1.68 Å while the structure of PGK from Campylobacter jejuni (CjPGK) has been determined at 2.14 Å resolution. The proteins' monomers are composed of two domains, each containing a Rossmann fold, hinged together by a helix which can be used to adjust the relative position between two domains. It is also shown that apo-forms of both BaPGK and CjPGK adopt open conformations as compared to the substrate and ATP bound forms of PGK from other species.

Original languageEnglish
Pages (from-to)15-26
Number of pages12
JournalJournal of Structural and Functional Genomics
Issue number1
StatePublished - Mar 2012
Externally publishedYes


  • Anthrax
  • Bacillus anthracis
  • Campylobacter jejuni
  • Carbohydrate degradation
  • Gastroenteritis
  • Glycolysis
  • Guillain-Barré syndrome
  • PGK
  • Pathogenic organism
  • Phosphoglycerate kinase
  • Rossmann fold


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