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J Struct Funct Genomics. 2012 Mar;13(1):15-26. doi: 10.1007/s10969-012-9131-9. Epub 2012 Mar 10.

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

Author information

1
Department of Molecular Physiology and Biological Physics, University of Virginia, 1340 Jefferson Park Avenue, Charlottesville, VA 22908, USA.

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.

PMID:
22403005
PMCID:
PMC4485498
DOI:
10.1007/s10969-012-9131-9
[Indexed for MEDLINE]
Free PMC Article

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