3tw0

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<StructureSection load='3tw0' size='340' side='right'caption='[[3tw0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3tw0' size='340' side='right'caption='[[3tw0]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tw0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae_(serotype_v) Streptococcus agalactiae (serotype v)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TW0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tw0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae_serogroup_V Streptococcus agalactiae serogroup V]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TW0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</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&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tvy|3tvy]], [[3txa|3txa]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAG0649 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=216466 Streptococcus agalactiae (serotype V)])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tw0 OCA], [https://pdbe.org/3tw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tw0 RCSB], [https://www.ebi.ac.uk/pdbsum/3tw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tw0 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=3tw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tw0 OCA], [https://pdbe.org/3tw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tw0 RCSB], [https://www.ebi.ac.uk/pdbsum/3tw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tw0 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q8E0S5_STRA5 Q8E0S5_STRA5]
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The crystal structure of a 75 kDa central fragment of GBS104, a tip pilin from the 2063V/R strain of Streptococcus agalactiae (group B streptococcus; GBS), is reported. In addition, a homology model of the remaining two domains of GBS104 was built and a model of full-length GBS104 was generated by combining the homology model (the N1 and N4 domains) and the crystal structure of the 75 kDa fragment (the N2 and N3 domains). This rod-shaped GBS104 model is constructed of three IgG-like domains (the N1, N2 and N4 domains) and one vWFA-like domain (the N3 domain). The N1 and N2 domains of GBS104 are assembled with distinct and remote segments contributed by the N- and C-termini. The metal-binding site in the N3 domain of GBS104 is in the closed/low-affinity conformation. Interestingly, this domain hosts two long arms that project away from the metal-binding site. Using site-directed mutagenesis, two cysteine residues that lock the N3 domain of GBS104 into the open/high-affinity conformation were introduced. Both wild-type and disulfide-locked recombinant proteins were tested for binding to extracellular matrix proteins such as collagen, fibronectin, fibrinogen and laminin, and an increase in fibronectin binding affinity was identified for the disulfide-locked N3 domain, suggesting that induced conformational changes may play a possible role in receptor binding.
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Structure of Streptococcus agalactiae tip pilin GBS104: a model for GBS pili assembly and host interactions.,Krishnan V, Dwivedi P, Kim BJ, Samal A, Macon K, Ma X, Mishra A, Doran KS, Ton-That H, Narayana SV Acta Crystallogr D Biol Crystallogr. 2013 Jun;69(Pt 6):1073-89. doi:, 10.1107/S0907444913004642. Epub 2013 May 15. PMID:23695252<ref>PMID:23695252</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3tw0" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Krishnan, V]]
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[[Category: Streptococcus agalactiae serogroup V]]
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[[Category: Narayana, S V.L]]
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[[Category: Krishnan V]]
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[[Category: Ancillary pilin]]
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[[Category: Narayana SVL]]
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[[Category: Cell adhesion]]
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[[Category: Gram-positive bacterial cell surface]]
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[[Category: Vwfa fold]]
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Revision as of 13:41, 14 March 2024

Structural Analysis of Adhesive Tip pilin, GBS104 from Group B Streptococcus agalactiae

PDB ID 3tw0

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