3Q3V
Crystal structure of Phosphoglycerate Kinase from Campylobacter jejuni.
Summary for 3Q3V
| Entry DOI | 10.2210/pdb3q3v/pdb |
| Descriptor | Phosphoglycerate kinase, POTASSIUM ION, FORMIC ACID, ... (6 entities in total) |
| Functional Keywords | structural genomics, center for structural genomics of infectious diseases, csgid, pgk, converts 3-phospho-d-glycerate to 3-phospho-d-glyceroyl phosphate during the glycolysis pathway, transferase |
| Biological source | Campylobacter jejuni subsp. jejuni NCTC 11168 |
| Cellular location | Cytoplasm : Q9PMQ5 |
| Total number of polymer chains | 2 |
| Total formula weight | 89614.08 |
| Authors | Filippova, E.V.,Wawrzak, Z.,Onopriyenko, O.,Edwards, A.,Savchenko, A.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2010-12-22, release date: 2011-01-12, Last modification date: 2024-11-06) |
| Primary citation | Zheng, H.,Filippova, E.V.,Tkaczuk, K.L.,Dworzynski, P.,Chruszcz, M.,Porebski, P.J.,Wawrzak, Z.,Onopriyenko, O.,Kudritska, M.,Grimshaw, S.,Savchenko, A.,Anderson, W.F.,Minor, W. Crystal structures of putative phosphoglycerate kinases from B. anthracis and C. jejuni. J.Struct.Funct.Genom., 13:15-26, 2012 Cited by PubMed 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. PubMed: 22403005DOI: 10.1007/s10969-012-9131-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.145 Å) |
Structure validation
Download full validation report
