1w6t: Difference between revisions

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


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==Crystal Structure Of Octameric Enolase From Streptococcus pneumoniae==
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<StructureSection load='1w6t' size='340' side='right'caption='[[1w6t]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
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</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>
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<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>
{{STRUCTURE_1w6t|  PDB=1w6t  |  SCENE=  }}
<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]]
Check<jmol>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/w6/1w6t_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1w6t ConSurf].
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== 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.


===CRYSTAL STRUCTURE OF OCTAMERIC ENOLASE FROM STREPTOCOCCUS PNEUMONIAE===
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<ref>PMID:15476816</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1w6t" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_15476816}}, adds the Publication Abstract to the page
*[[Enolase 3D structures|Enolase 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 15476816 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_15476816}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1W6T is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Streptococcus_pneumoniae Streptococcus pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W6T OCA].
[[Category: Streptococcus pneumoniae TIGR4]]
 
[[Category: Bergmann S]]
==Reference==
[[Category: Ehinger S]]
<ref group="xtra">PMID:15476816</ref><references group="xtra"/>
[[Category: Hammerschmidt S]]
[[Category: Phosphopyruvate hydratase]]
[[Category: Heinz DW]]
[[Category: Streptococcus pneumoniae]]
[[Category: Schubert W-D]]
[[Category: Bergmann, S.]]
[[Category: Ehinger, S.]]
[[Category: Hammerschmidt, S.]]
[[Category: Heinz, D W.]]
[[Category: Schubert, W D.]]
[[Category: Bacterial infection]]
[[Category: Glycolysis]]
[[Category: Lyase]]
[[Category: Moonlighting protein]]
[[Category: Phosphopyruvate hydratase]]
[[Category: Surface protein]]
 
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