|
|
(One intermediate revision not shown.) |
Line 1: |
Line 1: |
| | | |
| ==Crystal Structure of the laminin-binding protein Lbp of Streptococcus pyogenes== | | ==Crystal Structure of the laminin-binding protein Lbp of Streptococcus pyogenes== |
- | <StructureSection load='3gi1' size='340' side='right' caption='[[3gi1]], [[Resolution|resolution]] 2.45Å' scene=''> | + | <StructureSection load='3gi1' size='340' side='right'caption='[[3gi1]], [[Resolution|resolution]] 2.45Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3gi1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"micrococcus_scarlatinae"_klein_1884 "micrococcus scarlatinae" klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GI1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GI1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3gi1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes Streptococcus pyogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GI1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GI1 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 2.45Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lmb, lmb/spy_2007 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1314 "Micrococcus scarlatinae" Klein 1884])</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3gi1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gi1 OCA], [http://pdbe.org/3gi1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3gi1 RCSB], [http://www.ebi.ac.uk/pdbsum/3gi1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3gi1 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=3gi1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gi1 OCA], [https://pdbe.org/3gi1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gi1 RCSB], [https://www.ebi.ac.uk/pdbsum/3gi1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gi1 ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q99XV3_STRP1 Q99XV3_STRP1] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
Line 31: |
Line 33: |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Micrococcus scarlatinae klein 1884]] | + | [[Category: Large Structures]] |
- | [[Category: Baker, E N]] | + | [[Category: Streptococcus pyogenes]] |
- | [[Category: Caradoc-Davies, T T]] | + | [[Category: Baker EN]] |
- | [[Category: Linke, C]] | + | [[Category: Caradoc-Davies TT]] |
- | [[Category: Proft, T]] | + | [[Category: Linke C]] |
- | [[Category: Young, P G]] | + | [[Category: Proft T]] |
- | [[Category: Alpha/beta domain]]
| + | [[Category: Young PG]] |
- | [[Category: Helical backbone]]
| + | |
- | [[Category: Laminin-binding protein]]
| + | |
- | [[Category: Lbp]]
| + | |
- | [[Category: Metal transport]]
| + | |
- | [[Category: Metal-binding]]
| + | |
- | [[Category: Transport]]
| + | |
- | [[Category: Zinc-binding receptor]]
| + | |
| Structural highlights
Function
Q99XV3_STRP1
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The common pathogen Streptococcus pyogenes colonizes the human skin and tonsils and can invade underlying tissues. This requires the adhesion of S. pyogenes to host surface receptors mediated through adhesins. The laminin-binding protein Lbp has been suggested as an adhesin, specific for the human extracellular matrix protein laminin. Sequence alignments, however, indicate a relationship between Lbp and a family of bacterial metal-binding receptors. To further analyze the role of Lbp in S. pyogenes and its potential role in pathogenicity, Lbp has been crystallized, and its structure has been solved at a resolution of 2.45 A (R = 0.186; R(free) = 0.251). Lbp has the typical metal-binding receptor fold, comprising two globular (beta/alpha)(4) domains connected by a helical backbone. The two domains enclose the metal-binding site, which contains a zinc ion. The interaction of Lbp with laminin was further investigated and shown to be specific in vitro. Localization studies with antibodies specific for Lbp show that the protein is attached to the membrane. The data suggest that Lbp is primarily a zinc-binding protein, and we suggest that its interaction with laminin in vivo may be mediated via zinc bound to laminin.
The laminin-binding protein Lbp from Streptococcus pyogenes is a zinc receptor.,Linke C, Caradoc-Davies TT, Young PG, Proft T, Baker EN J Bacteriol. 2009 Sep;191(18):5814-23. Epub 2009 Jul 17. PMID:19617361[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Linke C, Caradoc-Davies TT, Young PG, Proft T, Baker EN. The laminin-binding protein Lbp from Streptococcus pyogenes is a zinc receptor. J Bacteriol. 2009 Sep;191(18):5814-23. Epub 2009 Jul 17. PMID:19617361 doi:10.1128/JB.00485-09
|