1w6t: Difference between revisions

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[[Image:1w6t.gif|left|200px]]
[[Image:1w6t.gif|left|200px]]


{{Structure
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|PDB= 1w6t |SIZE=350|CAPTION= <scene name='initialview01'>1w6t</scene>, resolution 2.10&Aring;
The line below this paragraph, containing "STRUCTURE_1w6t", creates the "Structure Box" on the page.
|SITE= <scene name='pdbsite=AC1:2pe+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] </span>
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|DOMAIN=
{{STRUCTURE_1w6t| PDB=1w6t  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w6t OCA], [http://www.ebi.ac.uk/pdbsum/1w6t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w6t RCSB]</span>
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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: bacterial infection]]
[[Category: Bacterial infection]]
[[Category: glycolysis]]
[[Category: Glycolysis]]
[[Category: lyase]]
[[Category: Lyase]]
[[Category: moonlighting protein]]
[[Category: Moonlighting protein]]
[[Category: phosphopyruvate hydratase]]
[[Category: Phosphopyruvate hydratase]]
[[Category: surface protein]]
[[Category: Surface protein]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:31:59 2008''

Revision as of 13:14, 3 May 2008

File:1w6t.gif

Template:STRUCTURE 1w6t

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

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