View source for 8sqx


==Solution structure of the basal pilin SpaB from Corynebacterium diphtheriae==
<StructureSection load='8sqx' size='340' side='right'caption='[[8sqx]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8sqx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_diphtheriae_NCTC_13129 Corynebacterium diphtheriae NCTC 13129]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8SQX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SQX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=8sqx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8sqx OCA], [https://pdbe.org/8sqx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8sqx RCSB], [https://www.ebi.ac.uk/pdbsum/8sqx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8sqx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6NF83_CORDI Q6NF83_CORDI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many species of pathogenic gram-positive bacteria display covalently crosslinked protein polymers (called pili or fimbriae) that mediate microbial adhesion to host tissues. These structures are assembled by pilus-specific sortase enzymes that join the pilin components together via lysine-isopeptide bonds. The archetypal SpaA pilus from Corynebacterium diphtheriae is built by the (Cd) SrtA pilus-specific sortase, which crosslinks lysine residues within the SpaA and SpaB pilins to build the shaft and base of the pilus, respectively. Here, we show that (Cd) SrtA crosslinks SpaB to SpaA via a K139(SpaB)-T494(SpaA) lysine-isopeptide bond. Despite sharing only limited sequence homology, an NMR structure of SpaB reveals striking similarities with the N-terminal domain of SpaA ((N) SpaA) that is also crosslinked by (Cd) SrtA. In particular, both pilins contain similarly positioned reactive lysine residues and adjacent disordered AB loops that are predicted to be involved in the recently proposed "latch" mechanism of isopeptide bond formation. Competition experiments using an inactive SpaB variant and additional NMR studies suggest that SpaB terminates SpaA polymerization by outcompeting (N) SpaA for access to a shared thioester enzyme-substrate reaction intermediate.

The basal and major pilins in the Corynebacterium diphtheriae SpaA pilus adopt similar structures that competitively react with the pilin polymerase.,Sue CK, Cheung NA, Mahoney BJ, McConnell SA, Scully JM, Fu JY, Chang C, Ton-That H, Loo JA, Clubb RT Biopolymers. 2023 May 25:e23539. doi: 10.1002/bip.23539. PMID:37227047<ref>PMID:37227047</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8sqx" style="background-color:#fffaf0;"></div>

==See Also==
*[[Pilin 3D structures|Pilin 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Corynebacterium diphtheriae NCTC 13129]]
[[Category: Large Structures]]
[[Category: Cheung NA]]
[[Category: Clubb RT]]
[[Category: Mahoney BJ]]
[[Category: Sue CK]]