View source for 3rkp


==Crystal structure of BcpA*(D312A), the major pilin subunit of Bacillus cereus==
<StructureSection load='3rkp' size='340' side='right'caption='[[3rkp]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3rkp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RKP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RKP 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]] 2.243&#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=3rkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rkp OCA], [https://pdbe.org/3rkp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rkp RCSB], [https://www.ebi.ac.uk/pdbsum/3rkp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rkp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q81D71_BACCR Q81D71_BACCR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacillus cereus strains elaborate pili on their surface using a mechanism of sortase-mediated cross-linking of major and minor pilus components. Here we used a combination of electron microscopy and atomic force microscopy to visualize these structures. Pili occur as single, double or higher order assemblies of filaments formed from monomers of the major pilin, BcpA, capped by the minor pilin, BcpB. Previous studies demonstrated that within assembled pili, four domains of BcpA - CNA(1) , CNA(2) , XNA and CNA(3) - each acquire intramolecular lysine-asparagine isopeptide bonds formed via catalytic glutamic acid or aspartic acid residues. Here we showed that mutants unable to form the intramolecular isopeptide bonds in the CNA(2) or CNA(3) domains retain the ability to form pilus bundles. A mutant lacking the CNA(1) isopeptide bond assembled deformed pilin subunits that failed to associate as bundles. X-ray crystallography revealed that the BcpA variant Asp(312) Ala, lacking an aspartyl catalyst, did not generate the isopeptide bond within the jelly-roll structure of XNA. The Asp(312) Ala mutant was also unable to form bundles and promoted the assembly of deformed pili. Thus, structural integrity of the CNA(1) and XNA domains are determinants for the association of pili into higher order bundle structures and determine native pilus structure.

Isopeptide bonds of the major pilin protein BcpA influence pilus structure and bundle formation on the surface of Bacillus cereus.,Hendrickx AP, Poor CB, Jureller JE, Budzik JM, He C, Schneewind O Mol Microbiol. 2012 Jul;85(1):152-63. doi: 10.1111/j.1365-2958.2012.08098.x. Epub, 2012 Jun 1. PMID:22624947<ref>PMID:22624947</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3rkp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Pilin 3D structures|Pilin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus cereus ATCC 14579]]
[[Category: Large Structures]]
[[Category: Budzik JM]]
[[Category: He C]]
[[Category: Hendrickx AP]]
[[Category: Jureller JE]]
[[Category: Poor CB]]
[[Category: Schneewind O]]