Journal of Structural and Functional Genomics

, Volume 13, Issue 1, pp 15–26

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
Short Communication

DOI: 10.1007/s10969-012-9131-9

Cite this article as:
Zheng, H., Filippova, E.V., Tkaczuk, K.L. et al. J Struct Funct Genomics (2012) 13: 15. doi:10.1007/s10969-012-9131-9

Abstract

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.

Keywords

Carbohydrate degradationGlycolysisPGKPhosphoglycerate kinasePathogenic organismAnthraxGastroenteritisGuillain–Barré syndromeRossmann foldBacillus anthracisCampylobacter jejuni

Abbreviations

BaPGK

Phosphoglycerate kinase from Bacillus anthracis

CjPGK

Phosphoglycerate kinase from Campylobacter jejuni

PGK

Phosphoglycerate kinase

ATP

Adenosine triphosphate

ADP

Adenosine diphosphate

3PG

3-Phospho-d-glycerate

SAXS

Small-angle X-ray scattering

ORF

Open reading frame

HEPES

2-[4-(2-Hydroxyethyl)piperazin-1-yl]ethanesulfonic acid

TCEP

Tris(2-carboxyethyl)phosphine-HCl

TEV

Tobacco etch virus

EDTA

Ethylenediaminetetraacetic acid

PEG

Polyethylene glycol

LS-CAT

Life Science Collaborative Access Team

EMBL

European Molecular Biology Laboratory

SAD

Single-wavelength anomalous diffraction

TLS

Translation/libration/screw

PDB

Protein Databank

RMSD

Root mean square deviation

GBS

Guillain–Barré syndrome

NIAID

National Institute of Allergy and Infectious Diseases

CSGID

Center of Structural Genomics for Infectious Disease

Copyright information

© Springer Science+Business Media B.V. 2012

Authors and Affiliations

  • Heping Zheng
    • 1
    • 5
  • Ekaterina V. Filippova
    • 2
    • 5
  • Karolina L. Tkaczuk
    • 1
    • 5
  • Piotr Dworzynski
    • 1
    • 5
  • Maksymilian Chruszcz
    • 1
    • 5
  • Przemyslaw J. Porebski
    • 1
    • 5
  • Zdzislaw Wawrzak
    • 5
    • 6
  • Olena Onopriyenko
    • 3
    • 5
  • Marina Kudritska
    • 3
    • 5
  • Sarah Grimshaw
    • 4
    • 5
  • Alexei Savchenko
    • 3
    • 5
  • Wayne F. Anderson
    • 2
    • 5
  • Wladek Minor
    • 1
    • 5
  1. 1.Department of Molecular Physiology and Biological PhysicsUniversity of VirginiaCharlottesvilleUSA
  2. 2.Department of Molecular Pharmacology and Biological ChemistryNorthwestern University Feinberg School of MedicineChicagoUSA
  3. 3.Banting and Best Department of Medical ResearchUniversity of TorontoTorontoCanada
  4. 4.J. Craig Venter InstituteRockvilleUSA
  5. 5.Center for Structural Genomics of Infectious Diseases (CSGID)
  6. 6.Northwestern UniversitySynchrotron Research CenterArgonneUSA