View source for 3zlb


==Crystal structure of phosphoglycerate kinase from Streptococcus pneumoniae==
<StructureSection load='3zlb' size='340' side='right'caption='[[3zlb]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zlb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_D39 Streptococcus pneumoniae D39]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZLB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.78&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=3zlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zlb OCA], [https://pdbe.org/3zlb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zlb RCSB], [https://www.ebi.ac.uk/pdbsum/3zlb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zlb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PGK_STRP2 PGK_STRP2] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Streptococcus pneumoniae is not only a commensal of the nasopharyngeal epithelium, but may also cause life-threatening diseases. Immune-electron microscopy studies revealed that the bacterial glycolytic enzyme, phosphoglycerate kinase (PGK), is localised on the pneumococcal surface of both encapsulated and non-capsulated strains and colocalises with plasminogen. Since pneumococci may concentrate host plasminogen (PLG) together with its activators on the bacterial cell surface to facilitate the formation of plasmin, the involvement of PGK in this process was studied. Specific binding of human or murine PLG to strain-independent PGK was documented, and surface plasmon resonance analyses indicated a high affinity interaction with the kringle domains 1-4 of PLG. Crystal structure determination of pneumococcal PGK together with peptide array analysis revealed localisation of PLG-binding site in the N-terminal region and provided structural motifs for the interaction with PLG. Based on structural analysis data, a potential interaction of PGK with tissue plasminogen activator (tPA) was proposed and experimentally confirmed by binding studies, plasmin activity assays and thrombus degradation analyses.

Pneumococcal phosphoglycerate kinase interacts with plasminogen and its tissue activator.,Fulde M, Bernardo-Garcia N, Rohde M, Nachtigall N, Frank R, Preissner KT, Klett J, Morreale A, Chhatwal GS, Hermoso JA, Bergmann S Thromb Haemost. 2013 Nov 7;111(3). PMID:24196407<ref>PMID:24196407</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zlb" style="background-color:#fffaf0;"></div>

==See Also==
*[[Phosphoglycerate kinase 3D structures|Phosphoglycerate kinase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptococcus pneumoniae D39]]
[[Category: Bernardo-Garcia N]]
[[Category: Hermoso JA]]