1W6T

Crystal Structure Of Octameric Enolase From Streptococcus pneumoniae

Summary for 1W6T

• Entry DOI: 10.2210/pdb1w6t/pdb
• Descriptor: ENOLASE, MAGNESIUM ION, NONAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: bacterial infection, surface protein, moonlighting protein, glycolysis, phosphopyruvate hydratase, lyase
• Biological source: STREPTOCOCCUS PNEUMONIAE (PNEUMOCOCCI)
• Cellular location: Cytoplasm: Q8DPS0
• Total number of polymer chains: 2
• Total formula weight: 97701.81

Authors

Ehinger, S.,Schubert, W.-D.,Bergmann, S.,Hammerschmidt, S.,Heinz, D.W. (deposition date: 2004-08-24, release date: 2005-08-22, Last modification date: 2023-12-13)

Primary citation

Ehinger, S.,Schubert, W.-D.,Bergmann, S.,Hammerschmidt, S.,Heinz, D.W.
Plasmin(Ogen)-Binding Alpha-Enolase from Streptococcus Pneumoniae: Crystal Structure and Evaluation of Plasmin(Ogen)-Binding Sites
J.Mol.Biol., 343:997-, 2004

PubMed Abstract: Alpha-enolases are ubiquitous cytoplasmic, glycolytic enzymes. In pathogenic bacteria, alpha-enolase doubles as a surface-displayed plasmin(ogen)-binder supporting virulence. The plasmin(ogen)-binding site was initially traced to the two C-terminal lysine residues. More recently, an internal nine-amino acid motif comprising residues 248 to 256 was identified with this function. We report the crystal structure of alpha-enolase from Streptococcus pneumoniae at 2.0A resolution, the first structure both of a plasminogen-binding and of an octameric alpha-enolase. While the dimer is structurally similar to other alpha-enolases, the octamer places the C-terminal lysine residues in an inaccessible, inter-dimer groove restricting the C-terminal lysine residues to a role in folding and oligomerization. The nine residue plasminogen-binding motif, by contrast, is exposed on the octamer surface revealing this as the primary site of interaction between alpha-enolase and plasminogen.

PubMed: 15476816
DOI: 10.1016/J.JMB.2004.08.088

Experimental method

X-RAY DIFFRACTION (2.1 Å)