1w6t: Difference between revisions
No edit summary |
No edit summary |
||
| Line 29: | Line 29: | ||
[[Category: surface protein]] | [[Category: surface protein]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:26:54 2007'' | ||
Revision as of 17:22, 30 October 2007
|
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 ... [(full description)]
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
Page seeded by OCA on Tue Oct 30 16:26:54 2007