4h0f
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4h0f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae_2603V/R Streptococcus agalactiae 2603V/R]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H0F FirstGlance]. <br> | <table><tr><td colspan='2'>[[4h0f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae_2603V/R Streptococcus agalactiae 2603V/R]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H0F FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.4Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4h0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h0f OCA], [https://pdbe.org/4h0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h0f RCSB], [https://www.ebi.ac.uk/pdbsum/4h0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h0f ProSAT]</span></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=4h0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h0f OCA], [https://pdbe.org/4h0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h0f RCSB], [https://www.ebi.ac.uk/pdbsum/4h0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h0f ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q8DZ80_STRA5 Q8DZ80_STRA5] | [https://www.uniprot.org/uniprot/Q8DZ80_STRA5 Q8DZ80_STRA5] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Lmb is a 34 kDa laminin binding surface adhesin of Streptococcus agalactiae. The structure of Lmb reported by us recently has shown that it consists of a metal binding crevice, in which a zinc ion is coordinated to three highly conserved histidines. To elucidate the structural and functional significance of the metal ion in Lmb, these histidines have been mutated to alanine and single, double and triple mutants were generated. These mutations resulted in insolubility of the protein and revealed altered secondary and tertiary structures, as evidenced by circular dichroism and fluorescence spectroscopy studies. The mutations also significantly decreased the binding affinity of Lmb to laminin, implicating the role played by the metal binding residues in maintaining the correct conformation of the protein for its binding to laminin. A highly disordered loop, proposed to be crucial for metal acquisition in homologous structures, was deleted in Lmb by mutation (DeltaLmb) and its crystal structure was solved at 2.6 A. The DeltaLmb structure was identical to the native Lmb structure with a bound zinc ion and exhibited laminin binding activity similar to wild type protein, suggesting that the loop might not have an important role in metal acquisition or adhesion in Lmb. Targeted mutations of histidine residues confirmed the importance of the zinc binding crevice for the structure and function of the Lmb adhesin. | ||
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| - | Metal binding is critical for the folding and function of laminin binding protein, Lmb of Streptococcus agalactiae.,Ragunathan P, Sridaran D, Weigel A, Shabayek S, Spellerberg B, Ponnuraj K PLoS One. 2013 Jun 24;8(6):e67517. doi: 10.1371/journal.pone.0067517. Print 2013. PMID:23826314<ref>PMID:23826314</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4h0f" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Mutant Structure of laminin-binding adhesin (Lmb) from Streptococcus agalactiae
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