3Q3V : Crystal structure of Phosphoglycerate Kinase from Campylobacter jejuni.

  • Ekaterina V. Filippova (Center for Structural Genomics of Infectious Diseases (CSGID) (Contributor)
  • Zdzislaw Wawrzak (Center for Structural Genomics of Infectious Diseases (CSGID) (Contributor)
  • Olena Onopriyenko (Contributor)
  • Alexei Savchenko (Contributor)
  • Wayne F Anderson (Contributor)



Experimental Technique/Method:X-RAY DIFFRACTION
Release Date:2011-01-12
Deposition Date:2010-12-22
Revision Date:2011-07-13#2012-05-09#2017-11-08
Molecular Weight:89614.08
Macromolecule Type:Protein
Residue Count:806
Atom Site Count:6093

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.
Date made available2011

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