1w6t
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CRYSTAL STRUCTURE OF OCTAMERIC ENOLASE FROM STREPTOCOCCUS PNEUMONIAE
OverviewOverview
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.
About this StructureAbout this Structure
1W6T is a Single protein structure of sequence from Streptococcus pneumoniae with MG and 2PE as ligands. Active as Phosphopyruvate hydratase, with EC number 4.2.1.11 Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: crystal structure and evaluation of plasmin(ogen)-binding sites., Ehinger S, Schubert WD, Bergmann S, Hammerschmidt S, Heinz DW, J Mol Biol. 2004 Oct 29;343(4):997-1005. PMID:15476816
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