6oq9: Difference between revisions

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-'''Unreleased structure'''
-The entry 6oq9 is ON HOLD
+==Solution structure of VEK50 in the bound form with plasminogen kringle 2==
+<StructureSection load='6oq9' size='340' side='right'caption='[[6oq9]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6oq9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OQ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OQ9 FirstGlance]. <br>
+</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=6oq9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oq9 OCA], [https://pdbe.org/6oq9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oq9 RCSB], [https://www.ebi.ac.uk/pdbsum/6oq9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oq9 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PAM_STRPY PAM_STRPY] Binds to human plasminogen (and plasmin) via its kringle repeats. Also binds to albumin, immunoglobulin G and fibrinogen. Could provide the bacteria with a mechanism for invasion, as streptococcal-bound plasmin could permit tissue penetration.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+VEK50 is a truncated peptide from a Streptococcal pyogenes surface human plasminogen (hPg) binding M-protein (PAM). VEK50 contains the full A-domain of PAM, which is responsible for its low nanomolar binding to hPg. The interaction of VEK50 with kringle 2, the PAM-binding domain in hPg (K2hPg), has been studied by high-resolution NMR spectroscopy. The data show that each VEK50 monomer in solution contains two tight binding sites for K2hPg, one each in the a1- (RH1; R(17)H(18)) and a2- (RH2; R(30)H(31)) repeats within the A-domain of VEK50. Two mutant forms of VEK50, viz., VEK50[RH1/AA] (VEK50(DeltaRH1)) and VEK50[RH2/AA] (VEK50(DeltaRH2)), were designed by replacing each RH with AA, thus eliminating one of the K2hPg binding sites within VEK50, and allowing separate study of each binding site. Using (13)C- and (15)N-labeled peptides, NMR-derived solution structures of VEK50 in its complex with K2hPg were solved. We conclude that the A-domain of PAM can accommodate two molecules of K2hPg docked within a short distance of each other, and the strength of the binding is slightly different for each site. The solution structure of the VEK50/K2hPg, complex, which is a reductionist model of the PAM/hPg complex, provides insights for the binding mechanism of PAM to a host protein, a process that is critical to S. pyogenes virulence.
-Authors: Yuan, Y., Castellino, F.J.
+Solution structural model of the complex of the binding regions of human plasminogen with its M-protein receptor from Streptococcus pyogenes.,Yuan Y, Ayinuola YA, Singh D, Ayinuola O, Mayfield JA, Quek A, Whisstock JC, Law RHP, Lee SW, Ploplis VA, Castellino FJ J Struct Biol. 2019 Jul 10. pii: S1047-8477(19)30154-6. doi:, 10.1016/j.jsb.2019.07.005. PMID:31301349<ref>PMID:31301349</ref>
-Description: Solution structure of VEK50 in the bound form with plasminogen kringle 2
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Yuan, Y]]
+<div class="pdbe-citations 6oq9" style="background-color:#fffaf0;"></div>
-[[Category: Castellino, F.J]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Streptococcus pyogenes]]
+[[Category: Castellino FJ]]
+[[Category: Yuan Y]]