View source for 6kyc


==Structure of the S207A mutant of Clostridium difficile sortase B==
<StructureSection load='6kyc' size='340' side='right'caption='[[6kyc]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6kyc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridioides_difficile_630 Clostridioides difficile 630]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KYC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KYC 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]] 2.604&#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=6kyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kyc OCA], [https://pdbe.org/6kyc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kyc RCSB], [https://www.ebi.ac.uk/pdbsum/6kyc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kyc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q183F3_CLOD6 Q183F3_CLOD6] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Most of Gram-positive bacteria anchor surface proteins to the peptidoglycan cell wall by sortase, a cysteine transpeptidase that targets proteins displaying a cell wall sorting signal. Unlike other bacteria, Clostridium difficile, the major human pathogen responsible for antibiotic-associated diarrhea, has only a single functional sortase (SrtB). Sortase's vital importance in bacterial virulence has been long recognized, and C. difficile sortase B (Cd-SrtB) has become an attractive therapeutic target for managing C. difficile infection (CDI). A better understanding of the molecular activity of Cd-SrtB may help spur the development of effective agents against CDI. In this study, using site-directed mutagenesis, biochemical and biophysical tools, LC-MS/MS, and crystallographic analyses, we identified key residues essential for Cd-SrtB catalysis and substrate recognition. To the best of our knowledge, we report first evidence that a conserved serine residue near the active site participates in the catalytic activity of Cd-SrtB and also SrtB from Staphylococcus aureus The serine residue indispensable for SrtB activity may be involved in stabilizing a thioacyl-enzyme intermediate because it is neither a nucleophilic residue nor a substrate-interacting residue, based on the LC-MS/MS data and available structural models of SrtB-substrate complexes. Furthermore, we also demonstrated that residues 163-168 located on the beta6/beta7 loop of Cd-SrtB dominate specific recognition of the peptide substrate PPKTG. The results of this work reveal key residues with roles in catalysis and substrate specificity of Cd-SrtB.

Functional analysis of Clostridium difficile sortase B reveals key residues for catalytic activity and substrate specificity.,Kang CY, Huang IH, Chou CC, Wu TY, Chang JC, Hsiao YY, Cheng CH, Tsai WJ, Hsu KC, Wang S J Biol Chem. 2020 Jan 31. pii: RA119.011322. doi: 10.1074/jbc.RA119.011322. PMID:32005667<ref>PMID:32005667</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6kyc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridioides difficile 630]]
[[Category: Large Structures]]
[[Category: Chang JC]]
[[Category: Cheng CH]]
[[Category: Hsiao YY]]
[[Category: Hsu KC]]
[[Category: Huang IH]]
[[Category: Kang CY]]
[[Category: Tsai WJ]]
[[Category: Wang SY]]
[[Category: Wu TY]]