View source for 8wt4


==Crystal structure of DL-endopeptidase CwlO complexed with IseA==
<StructureSection load='8wt4' size='340' side='right'caption='[[8wt4]], [[Resolution|resolution]] 1.62&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8wt4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8WT4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8WT4 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]] 1.62&#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=8wt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wt4 OCA], [https://pdbe.org/8wt4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wt4 RCSB], [https://www.ebi.ac.uk/pdbsum/8wt4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wt4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/YOEB_BACSU YOEB_BACSU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peptidoglycan DL-endopeptidases locally cleave the peptide stem of peptidoglycan in the bacterial cell wall. This process facilitates bacterial growth and division by loosening the rigid peptidoglycan layer. IseA binds to the active site of multiple DL-endopeptidases and inhibits excessive peptidoglycan degradation that leads to cell lysis. To better understand how IseA inhibits DL-endopeptidase activity, we determined the crystal structure of the peptidoglycan DL-endopeptidase CwlO/IseA complex and compared it with that of the peptidoglycan DL-endopeptidase LytE/IseA complex. Structural analyses showed significant differences between the hydrophobic pocket-binding residues of the DL-endopeptidases (F361 of CwlO and W237 of LytE). Additionally, binding assays showed that the F361 mutation of CwlO to the bulkier hydrophobic residue, tryptophan, increased its binding affinity for IseA, whereas mutation to alanine reduced the affinity. These analyses revealed that the hydrophobic pocket-binding residue of DL-endopeptidases determines IseA-binding affinity and is required for substrate-mimetic inhibition by IseA.

Structural analysis of the peptidoglycan DL-endopeptidase CwlO complexed with its inhibitory protein IseA.,Tandukar S, Kwon E, Kim DY FEBS J. 2024 Jun 5. doi: 10.1111/febs.17197. PMID:38840475<ref>PMID:38840475</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8wt4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Large Structures]]
[[Category: Kim DY]]
[[Category: Kwon E]]
[[Category: Tandukar S]]