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6kyc
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the S207A mutant of Clostridium difficile sortase B== | |
| + | <StructureSection load='6kyc' size='340' side='right'caption='[[6kyc]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6kyc]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KYC FirstGlance]. <br> | ||
| + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gyj|5gyj]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6kyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kyc OCA], [http://pdbe.org/6kyc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kyc RCSB], [http://www.ebi.ac.uk/pdbsum/6kyc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kyc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6kyc" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chang, J C]] | ||
| + | [[Category: Cheng, C H]] | ||
| + | [[Category: Hsiao, Y Y]] | ||
| + | [[Category: Hsu, K C]] | ||
| + | [[Category: Huang, I H]] | ||
| + | [[Category: Kang, C Y]] | ||
| + | [[Category: Tsai, W J]] | ||
| + | [[Category: Wang, S Y]] | ||
| + | [[Category: Wu, T Y]] | ||
| + | [[Category: Clostridium difficile]] | ||
| + | [[Category: Cysteine transpeptidase]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Sortase b]] | ||
Revision as of 06:21, 19 February 2020
Structure of the S207A mutant of Clostridium difficile sortase B
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