3zlb

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{{STRUCTURE_3zlb| PDB=3zlb | SCENE= }}
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==Crystal structure of phosphoglycerate kinase from Streptococcus pneumoniae==
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===Crystal structure of phosphoglycerate kinase from Streptococcus pneumoniae===
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<StructureSection load='3zlb' size='340' side='right' caption='[[3zlb]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
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{{ABSTRACT_PUBMED_24196407}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3zlb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strp2 Strp2]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZLB FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglycerate_kinase Phosphoglycerate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.3 2.7.2.3] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3zlb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zlb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zlb RCSB], [http://www.ebi.ac.uk/pdbsum/3zlb PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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==About this Structure==
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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>
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[[3zlb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZLB OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:024196407</ref><references group="xtra"/><references/>
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</div>
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==See Also==
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*[[Phosphoglycerate Kinase|Phosphoglycerate Kinase]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Phosphoglycerate kinase]]
[[Category: Phosphoglycerate kinase]]
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[[Category: Bernardo-Garcia, N.]]
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[[Category: Strp2]]
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[[Category: Hermoso, J A.]]
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[[Category: Bernardo-Garcia, N]]
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[[Category: Hermoso, J A]]
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 12:30, 5 January 2015

Crystal structure of phosphoglycerate kinase from Streptococcus pneumoniae

3zlb, resolution 1.78Å

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