View source for 5xcc


==X-ray structure of Clostridium perfringens pili protein CppA==
<StructureSection load='5xcc' size='340' side='right'caption='[[5xcc]], [[Resolution|resolution]] 2.48&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xcc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens_str._13 Clostridium perfringens str. 13]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XCC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XCC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.48&#8491;</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=5xcc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xcc OCA], [https://pdbe.org/5xcc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xcc RCSB], [https://www.ebi.ac.uk/pdbsum/5xcc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xcc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8XP10_CLOPE Q8XP10_CLOPE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pili in Gram-positive bacteria are flexible rod proteins associated with the bacterial cell surface, and they play important roles in the initial adhesion to host tissues and colonization. The pilus shaft is formed by the covalent polymerization of major pilins, catalyzed by sortases, a family of cysteine transpeptidases. Here, X-ray structures of the major pilins from Clostridium perfringens strains 13 and SM101 and of sortase from strain SM101 are presented with biochemical analysis to detect the formation of pili in vivo. The major pilin from strain 13 adopts an elongated structure to form noncovalently linked polymeric chains in the crystal, yielding a practical model of the pilus fiber structure. The major pilin from strain SM101 adopts a novel bent structure and associates to form a left-handed twist like an antiparallel double helix in the crystal, which is likely to promote bacterial cell-cell interactions. A modeling study showed that pilin with a bent structure interacts favorably with sortase. The major pilin from strain SM101 was considered to be in an equilibrium state between an elongated and a bent structure through dynamic conformational change, which may be involved in pili-mediated colonization and sortase-mediated polymerization of pili.

Structures of major pilins in Clostridium perfringens demonstrate dynamic conformational change.,Tamai E, Katayama S, Sekiya H, Nariya H, Kamitori S Acta Crystallogr D Struct Biol. 2019 Aug 1;75(Pt 8):718-732. doi:, 10.1107/S2059798319009689. Epub 2019 Jul 30. PMID:31373571<ref>PMID:31373571</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xcc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Clostridium perfringens str. 13]]
[[Category: Large Structures]]
[[Category: Kamitori S]]
[[Category: Tamai E]]