1w6t: Difference between revisions
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'''CRYSTAL STRUCTURE OF OCTAMERIC ENOLASE FROM STREPTOCOCCUS PNEUMONIAE''' | '''CRYSTAL STRUCTURE OF OCTAMERIC ENOLASE FROM STREPTOCOCCUS PNEUMONIAE''' | ||
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[[Category: Heinz, D W.]] | [[Category: Heinz, D W.]] | ||
[[Category: Schubert, W D.]] | [[Category: Schubert, W D.]] | ||
[[Category: | [[Category: Bacterial infection]] | ||
[[Category: | [[Category: Glycolysis]] | ||
[[Category: | [[Category: Lyase]] | ||
[[Category: | [[Category: Moonlighting protein]] | ||
[[Category: | [[Category: Phosphopyruvate hydratase]] | ||
[[Category: | [[Category: Surface protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:14:11 2008'' | |||
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Revision as of 13:14, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 13:14:11 2008