3pay

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<StructureSection load='3pay' size='340' side='right'caption='[[3pay]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='3pay' size='340' side='right'caption='[[3pay]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3pay]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Baco1 Baco1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PAY FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3pay]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_ovatus_ATCC_8483 Bacteroides ovatus ATCC 8483]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PAY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PAY 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=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 2.5&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BACOVA_04077 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=411476 BACO1])</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=3pay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pay OCA], [https://pdbe.org/3pay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pay RCSB], [https://www.ebi.ac.uk/pdbsum/3pay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pay 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=3pay FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pay OCA], [https://pdbe.org/3pay PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pay RCSB], [https://www.ebi.ac.uk/pdbsum/3pay PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pay 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/A7M1U3_BACO1 A7M1U3_BACO1]
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Pili are proteinaceous polymers of linked pilins that protrude from the cell surface of many bacteria and often mediate adherence and virulence. We investigated a set of 20 Bacteroidia pilins from the human microbiome whose structures and mechanism of assembly were unknown. Crystal structures and biochemical data revealed a diverse protein superfamily with a common Greek-key beta sandwich fold with two transthyretin-like repeats that polymerize into a pilus through a strand-exchange mechanism. The assembly mechanism of the central, structural pilins involves proteinase-assisted removal of their N-terminal beta strand, creating an extended hydrophobic groove that binds the C-terminal donor strands of the incoming pilin. Accessory pilins at the tip and base have unique structural features specific to their location, allowing initiation or termination of the assembly. The Bacteroidia pilus, therefore, has a biogenesis mechanism that is distinct from other known pili and likely represents a different type of bacterial pilus.
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A Distinct Type of Pilus from the Human Microbiome.,Xu Q, Shoji M, Shibata S, Naito M, Sato K, Elsliger MA, Grant JC, Axelrod HL, Chiu HJ, Farr CL, Jaroszewski L, Knuth MW, Deacon AM, Godzik A, Lesley SA, Curtis MA, Nakayama K, Wilson IA Cell. 2016 Apr 21;165(3):690-703. doi: 10.1016/j.cell.2016.03.016. Epub 2016 Apr , 7. PMID:27062925<ref>PMID:27062925</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 3pay" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Baco1]]
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[[Category: Bacteroides ovatus ATCC 8483]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Structural genomic]]
 
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[[Category: Cell adhesion]]
 
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[[Category: Jcsg]]
 
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[[Category: PSI, Protein structure initiative]]
 
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[[Category: Psi-biology]]
 

Revision as of 13:30, 1 March 2024

Crystal structure of a putative adhesin (BACOVA_04077) from Bacteroides ovatus at 2.50 A resolution

PDB ID 3pay

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