3phs

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Current revision (13:31, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3phs' size='340' side='right'caption='[[3phs]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3phs' size='340' side='right'caption='[[3phs]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3phs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Stra5 Stra5]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2pz4 2pz4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PHS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3phs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae_2603V/R Streptococcus agalactiae 2603V/R]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2pz4 2pz4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PHS FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3pf2|3pf2]]</div></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]] 1.8&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GBS052, SAG0646 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208435 STRA5])</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=3phs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3phs OCA], [https://pdbe.org/3phs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3phs RCSB], [https://www.ebi.ac.uk/pdbsum/3phs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3phs 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=3phs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3phs OCA], [https://pdbe.org/3phs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3phs RCSB], [https://www.ebi.ac.uk/pdbsum/3phs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3phs 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/Q8E0S8_STRA5 Q8E0S8_STRA5]
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Streptococcus agalactiae is the leading cause of neonatal pneumonia, sepsis, and meningitis. The pathogen assembles heterotrimeric pilus structures on its surface; however, their function in pathogenesis is poorly understood. We report here the crystal structure of the pilin GBS52, which reveals two IgG-like fold domains, N1 and N2. Each domain is comprised of seven antiparallel beta strands, an arrangement similar to the fold observed in the Staphylococcus aureus adhesin Cna. Consistent with its role as an adhesin, deletion of gbs52 gene significantly reduces bacterial adherence to pulmonary epithelial cells. Moreover, latex beads linked to the GBS52 protein adhere to pulmonary but not to many other epithelial cells; binding to the former is specifically inhibited by antibodies against GBS52. Nonetheless, substantial binding is only observed with N2 domain-conjugated beads. This study presents the structure of a Gram-positive pilin that utilizes a distinct IgG fold variant to mediate pathogen adherence to a specific tissue.
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An IgG-like domain in the minor pilin GBS52 of Streptococcus agalactiae mediates lung epithelial cell adhesion.,Krishnan V, Gaspar AH, Ye N, Mandlik A, Ton-That H, Narayana SV Structure. 2007 Aug;15(8):893-903. PMID:17697995<ref>PMID:17697995</ref>
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==See Also==
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*[[Pilin 3D structures|Pilin 3D structures]]
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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 3phs" 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: Stra5]]
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[[Category: Streptococcus agalactiae 2603V/R]]
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[[Category: Krishnan, V]]
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[[Category: Krishnan V]]
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[[Category: Narayana, S V.L]]
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[[Category: Narayana SVL]]
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[[Category: Adhesion]]
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[[Category: Cell adhesion]]
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[[Category: Cell ahdesion]]
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[[Category: Cell wall anchoring]]
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[[Category: Gbs52]]
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[[Category: Gram-positive bacterial cell wall]]
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[[Category: Gram-positive pilin]]
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[[Category: Ig-like fold]]
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[[Category: Igg-rev fold]]
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[[Category: Isopeptide bond]]
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[[Category: Pilus subunit]]
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[[Category: Streptococcus agalactiae]]
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[[Category: Structural protein]]
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Current revision

Crystal Structure of GBS52, the minor pilin in gram-positive pathogen Streptococcus agalactiae

PDB ID 3phs

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OCA

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