4mcu: Difference between revisions
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==Crystal structure of disulfide oxidoreductase from Klebsiella pneumoniae in reduced state== | ==Crystal structure of disulfide oxidoreductase from Klebsiella pneumoniae in reduced state== | ||
<StructureSection load='4mcu' size='340' side='right' caption='[[4mcu]], [[Resolution|resolution]] 1.99Å' scene=''> | <StructureSection load='4mcu' size='340' side='right'caption='[[4mcu]], [[Resolution|resolution]] 1.99Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4mcu]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4mcu]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae_342 Klebsiella pneumoniae 342]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MCU FirstGlance]. <br> | ||
</td></tr> | </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=4mcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mcu OCA], [https://pdbe.org/4mcu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mcu RCSB], [https://www.ebi.ac.uk/pdbsum/4mcu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mcu ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/B5XZJ6_KLEP3 B5XZJ6_KLEP3] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4mcu" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4mcu" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Protein disulfide oxidoreductase|Protein disulfide oxidoreductase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Klebsiella pneumoniae 342]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Kurth F]] | ||
[[Category: | [[Category: Martin JL]] | ||
[[Category: | [[Category: Premkumar L]] | ||
Revision as of 14:10, 21 December 2022
Crystal structure of disulfide oxidoreductase from Klebsiella pneumoniae in reduced stateCrystal structure of disulfide oxidoreductase from Klebsiella pneumoniae in reduced state
Structural highlights
FunctionPublication Abstract from PubMedBacterial DsbA enzymes catalyze oxidative folding of virulence factors, and have been identified as targets for antivirulence drugs. However, DsbA enzymes characterized to date exhibit a wide spectrum of redox properties and divergent structural features compared to the prototypical DsbA enzyme of Escherichia coli DsbA (EcDsbA). Nonetheless, sequence analysis shows that DsbAs are more highly conserved than their known substrate virulence factors, highlighting the potential to inhibit virulence across a range of organisms by targeting DsbA. For example, Salmonella enterica typhimurium (SeDsbA, 86 % sequence identity to EcDsbA) shares almost identical structural, surface and redox properties. Using comparative sequence and structure analysis we predicted that five other bacterial DsbAs would share these properties. To confirm this, we characterized Klebsiella pneumoniae DsbA (KpDsbA, 81 % identity to EcDsbA). As expected, the redox properties, structure and surface features (from crystal and NMR data) of KpDsbA were almost identical to those of EcDsbA and SeDsbA. Moreover, KpDsbA and EcDsbA bind peptides derived from their respective DsbBs with almost equal affinity, supporting the notion that compounds designed to inhibit EcDsbA will also inhibit KpDsbA. Taken together, our data show that DsbAs fall into different classes; that DsbAs within a class may be predicted by sequence analysis of binding loops; that DsbAs within a class are able to complement one another in vivo and that compounds designed to inhibit EcDsbA are likely to inhibit DsbAs within the same class. Comparative Sequence, Structure and Redox Analyses of Klebsiella pneumoniae DsbA Show That Anti-Virulence Target DsbA Enzymes Fall into Distinct Classes.,Kurth F, Rimmer K, Premkumar L, Mohanty B, Duprez W, Halili MA, Shouldice SR, Heras B, Fairlie DP, Scanlon MJ, Martin JL PLoS One. 2013 Nov 14;8(11):e80210. doi: 10.1371/journal.pone.0080210. PMID:24244651[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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