1w6t
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Alpha-enolases are ubiquitous cytoplasmic, glycolytic enzymes. In | + | 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 Structure== | ==About this Structure== | ||
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[[Category: Ehinger, S.]] | [[Category: Ehinger, S.]] | ||
[[Category: Hammerschmidt, S.]] | [[Category: Hammerschmidt, S.]] | ||
| - | [[Category: Heinz, D | + | [[Category: Heinz, D W.]] |
| - | [[Category: Schubert, W | + | [[Category: Schubert, W D.]] |
[[Category: 2PE]] | [[Category: 2PE]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: surface protein]] | [[Category: surface protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:04 2008'' |
Revision as of 13:41, 21 February 2008
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CRYSTAL STRUCTURE OF OCTAMERIC ENOLASE FROM STREPTOCOCCUS PNEUMONIAE
Overview
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 Structure
1W6T is a Single protein structure of sequence from Streptococcus pneumoniae with and as ligands. Active as Phosphopyruvate hydratase, with EC number 4.2.1.11 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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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