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1w6t

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Crystal Structure Of Octameric Enolase From Streptococcus pneumoniae

Structural highlights

1w6t is a 2 chain structure with sequence from Streptococcus pneumoniae TIGR4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.1Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ENO_STRPN Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. Binds plasminogen when expressed at the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity, which in turn contributes to the degradation of the extracellular matrix and transmigration of the bacteria.[HAMAP-Rule:MF_00318]^[1] ^[2] ^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bergmann S, Rohde M, Chhatwal GS, Hammerschmidt S. alpha-Enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface. Mol Microbiol. 2001 Jun;40(6):1273-87. PMID:11442827 doi:10.1046/j.1365-2958.2001.02448.x
↑ Whiting GC, Evans JT, Patel S, Gillespie SH. Purification of native alpha-enolase from Streptococcus pneumoniae that binds plasminogen and is immunogenic. J Med Microbiol. 2002 Oct;51(10):837-843. PMID:12435062 doi:10.1099/0022-1317-51-10-837
↑ Bergmann S, Rohde M, Preissner KT, Hammerschmidt S. The nine residue plasminogen-binding motif of the pneumococcal enolase is the major cofactor of plasmin-mediated degradation of extracellular matrix, dissolution of fibrin and transmigration. Thromb Haemost. 2005 Aug;94(2):304-11. PMID:16113819 doi:10.1160/TH05-05-0369
↑ Ehinger S, Schubert WD, Bergmann S, Hammerschmidt S, Heinz DW. Plasmin(ogen)-binding alpha-enolase from Streptococcus pneumoniae: crystal structure and evaluation of plasmin(ogen)-binding sites. J Mol Biol. 2004 Oct 29;343(4):997-1005. PMID:15476816 doi:10.1016/j.jmb.2004.08.088

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1w6t"

@@ Line 3: / Line 3: @@
 <StructureSection load='1w6t' size='340' side='right'caption='[[1w6t]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1w6t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Strpn Strpn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W6T FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1w6t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_TIGR4 Streptococcus pneumoniae TIGR4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W6T FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphopyruvate_hydratase Phosphopyruvate hydratase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.11 4.2.1.11] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w6t OCA], [https://pdbe.org/1w6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w6t RCSB], [https://www.ebi.ac.uk/pdbsum/1w6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w6t ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/ENO_STRPN ENO_STRPN] Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. Binds plasminogen when expressed at the bacterial cell surface, potentially allowing the bacterium to acquire surface-associated proteolytic activity, which in turn contributes to the degradation of the extracellular matrix and transmigration of the bacteria.[HAMAP-Rule:MF_00318]<ref>PMID:11442827</ref> <ref>PMID:12435062</ref> <ref>PMID:16113819</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 37: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Phosphopyruvate hydratase]]
+[[Category: Streptococcus pneumoniae TIGR4]]
-[[Category: Strpn]]
+[[Category: Bergmann S]]
-[[Category: Bergmann, S]]
+[[Category: Ehinger S]]
-[[Category: Ehinger, S]]
+[[Category: Hammerschmidt S]]
-[[Category: Hammerschmidt, S]]
+[[Category: Heinz DW]]
-[[Category: Heinz, D W]]
+[[Category: Schubert W-D]]
-[[Category: Schubert, W D]]
-[[Category: Bacterial infection]]
-[[Category: Glycolysis]]
-[[Category: Lyase]]
-[[Category: Moonlighting protein]]
-[[Category: Surface protein]]

1w6t

From Proteopedia

Current revision

Crystal Structure Of Octameric Enolase From Streptococcus pneumoniae

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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