3ZLB
Crystal structure of phosphoglycerate kinase from Streptococcus pneumoniae
Summary for 3ZLB
| Entry DOI | 10.2210/pdb3zlb/pdb |
| Descriptor | PHOSPHOGLYCERATE KINASE, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total) |
| Functional Keywords | transferase |
| Biological source | STREPTOCOCCUS PNEUMONIAE |
| Total number of polymer chains | 1 |
| Total formula weight | 42957.45 |
| Authors | Bernardo-Garcia, N.,Hermoso, J.A. (deposition date: 2013-01-30, release date: 2014-02-12, Last modification date: 2023-12-20) |
| Primary citation | Fulde, M.,Bernardo-Garcia, N.,Rohde, M.,Nachtigall, N.,Frank, R.,Preissner, K.T.,Klett, J.,Morreale, A.,Chhatwal, G.S.,Hermoso, J.A.,Bergmann, S. Pneumococcal phosphoglycerate kinase interacts with plasminogen and its tissue activator. Thromb. Haemost., 111:401-416, 2014 Cited by PubMed Abstract: Streptococcus pneumoniae is not only a commensal of the nasopharyngeal epithelium, but may also cause life-threatening diseases. Immune-electron microscopy studies revealed that the bacterial glycolytic enzyme, phosphoglycerate kinase (PGK), is localised on the pneumococcal surface of both capsulated and non-capsulated strains and colocalises with plasminogen. Since pneumococci may concentrate host plasminogen (PLG) together with its activators on the bacterial cell surface to facilitate the formation of plasmin, the involvement of PGK in this process was studied. Specific binding of human or murine PLG to strain-independent PGK was documented, and surface plasmon resonance analyses indicated a high affinity interaction with the kringle domains 1-4 of PLG. Crystal structure determination of pneumococcal PGK together with peptide array analysis revealed localisation of PLG-binding site in the N-terminal region and provided structural motifs for the interaction with PLG. Based on structural analysis data, a potential interaction of PGK with tissue plasminogen activator (tPA) was proposed and experimentally confirmed by binding studies, plasmin activity assays and thrombus degradation analyses. PubMed: 24196407DOI: 10.1160/TH13-05-0421 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.78 Å) |
Structure validation
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